Crystal structure and functional implications of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases

Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria; however, the synthesis mechanism remains elusive. Here, we determine the high-resolution structures of cyclic di-pyrimidine-synthesizing c GAS/ D ncV-l...

Full description

Saved in:
Bibliographic Details
Published inNature communications Vol. 14; no. 1; p. 5078
Main Authors Yang, Chia-Shin, Ko, Tzu-Ping, Chen, Chao-Jung, Hou, Mei-Hui, Wang, Yu-Chuan, Chen, Yeh
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 21.08.2023
Nature Publishing Group
Nature Portfolio
Subjects
140/58
631/326/41/2536
631/45/607
631/535/1266
Bacteria
Crystal structure
Cytosine
Humanities and Social Sciences
multidisciplinary
Nucleotides
Phages
Proteins
Pyrimidines
Science
Science (multidisciplinary)
Second messengers
Structural analysis
Structure-function relationships
Substrates
Synthesis
Uracil
Online AccessGet full text

Cover

Abstract Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria; however, the synthesis mechanism remains elusive. Here, we determine the high-resolution structures of cyclic di-pyrimidine-synthesizing c GAS/ D ncV-like n ucleotidyl t ransferases (CD-NTases) in clade E (CdnE) in its apo, substrate-, and intermediate-bound states. A conserved (R/Q)xW motif controlling the pyrimidine specificity of donor nucleotide is identified. Mutation of Trp or Arg from the (R/Q)xW motif to Ala rewires its specificity to purine nucleotides, producing mixed purine-pyrimidine cyclic dinucleotides (CDNs). Preferential binding of uracil over cytosine bases explains the product specificity of cyclic di-pyrimidine-synthesizing CdnE to cyclic di-UMP (cUU). Based on the intermediate-bound structures, a synthetic pathway for cUU containing a unique 2’3’-phosphodiester linkage through intermediate pppU[3’−5’]pU is deduced. Our results provide a framework for pyrimidine selection and establish the importance of conserved residues at the C-terminal loop for the specificity determination of CD-NTases. Here, the authors present structural and functional characterization of bacterial CD-NTases that synthesize cyclic dipyrimidines for phage resistance, revealing a (R/Q)xW motif dictating pyrimidine selection which suggests a sequential pathway for synthesizing 2’3’-cyclic di-UMP.
AbstractList Abstract Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria; however, the synthesis mechanism remains elusive. Here, we determine the high-resolution structures of cyclic di-pyrimidine-synthesizing c GAS/ D ncV-like n ucleotidyl t ransferases (CD-NTases) in clade E (CdnE) in its apo, substrate-, and intermediate-bound states. A conserved (R/Q)xW motif controlling the pyrimidine specificity of donor nucleotide is identified. Mutation of Trp or Arg from the (R/Q)xW motif to Ala rewires its specificity to purine nucleotides, producing mixed purine-pyrimidine cyclic dinucleotides (CDNs). Preferential binding of uracil over cytosine bases explains the product specificity of cyclic di-pyrimidine-synthesizing CdnE to cyclic di-UMP (cUU). Based on the intermediate-bound structures, a synthetic pathway for cUU containing a unique 2’3’-phosphodiester linkage through intermediate pppU[3’−5’]pU is deduced. Our results provide a framework for pyrimidine selection and establish the importance of conserved residues at the C-terminal loop for the specificity determination of CD-NTases.
Abstract Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria; however, the synthesis mechanism remains elusive. Here, we determine the high-resolution structures of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases (CD-NTases) in clade E (CdnE) in its apo, substrate-, and intermediate-bound states. A conserved (R/Q)xW motif controlling the pyrimidine specificity of donor nucleotide is identified. Mutation of Trp or Arg from the (R/Q)xW motif to Ala rewires its specificity to purine nucleotides, producing mixed purine-pyrimidine cyclic dinucleotides (CDNs). Preferential binding of uracil over cytosine bases explains the product specificity of cyclic di-pyrimidine-synthesizing CdnE to cyclic di-UMP (cUU). Based on the intermediate-bound structures, a synthetic pathway for cUU containing a unique 2’3’-phosphodiester linkage through intermediate pppU[3’−5’]pU is deduced. Our results provide a framework for pyrimidine selection and establish the importance of conserved residues at the C-terminal loop for the specificity determination of CD-NTases.
Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria; however, the synthesis mechanism remains elusive. Here, we determine the high-resolution structures of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases (CD-NTases) in clade E (CdnE) in its apo, substrate-, and intermediate-bound states. A conserved (R/Q)xW motif controlling the pyrimidine specificity of donor nucleotide is identified. Mutation of Trp or Arg from the (R/Q)xW motif to Ala rewires its specificity to purine nucleotides, producing mixed purine-pyrimidine cyclic dinucleotides (CDNs). Preferential binding of uracil over cytosine bases explains the product specificity of cyclic di-pyrimidine-synthesizing CdnE to cyclic di-UMP (cUU). Based on the intermediate-bound structures, a synthetic pathway for cUU containing a unique 2'3'-phosphodiester linkage through intermediate pppU[3'-5']pU is deduced. Our results provide a framework for pyrimidine selection and establish the importance of conserved residues at the C-terminal loop for the specificity determination of CD-NTases.
Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria; however, the synthesis mechanism remains elusive. Here, we determine the high-resolution structures of cyclic di-pyrimidine-synthesizing c GAS/ D ncV-like n ucleotidyl t ransferases (CD-NTases) in clade E (CdnE) in its apo, substrate-, and intermediate-bound states. A conserved (R/Q)xW motif controlling the pyrimidine specificity of donor nucleotide is identified. Mutation of Trp or Arg from the (R/Q)xW motif to Ala rewires its specificity to purine nucleotides, producing mixed purine-pyrimidine cyclic dinucleotides (CDNs). Preferential binding of uracil over cytosine bases explains the product specificity of cyclic di-pyrimidine-synthesizing CdnE to cyclic di-UMP (cUU). Based on the intermediate-bound structures, a synthetic pathway for cUU containing a unique 2’3’-phosphodiester linkage through intermediate pppU[3’−5’]pU is deduced. Our results provide a framework for pyrimidine selection and establish the importance of conserved residues at the C-terminal loop for the specificity determination of CD-NTases. Here, the authors present structural and functional characterization of bacterial CD-NTases that synthesize cyclic dipyrimidines for phage resistance, revealing a (R/Q)xW motif dictating pyrimidine selection which suggests a sequential pathway for synthesizing 2’3’-cyclic di-UMP.
Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria; however, the synthesis mechanism remains elusive. Here, we determine the high-resolution structures of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases (CD-NTases) in clade E (CdnE) in its apo, substrate-, and intermediate-bound states. A conserved (R/Q)xW motif controlling the pyrimidine specificity of donor nucleotide is identified. Mutation of Trp or Arg from the (R/Q)xW motif to Ala rewires its specificity to purine nucleotides, producing mixed purine-pyrimidine cyclic dinucleotides (CDNs). Preferential binding of uracil over cytosine bases explains the product specificity of cyclic di-pyrimidine-synthesizing CdnE to cyclic di-UMP (cUU). Based on the intermediate-bound structures, a synthetic pathway for cUU containing a unique 2’3’-phosphodiester linkage through intermediate pppU[3’−5’]pU is deduced. Our results provide a framework for pyrimidine selection and establish the importance of conserved residues at the C-terminal loop for the specificity determination of CD-NTases.Here, the authors present structural and functional characterization of bacterial CD-NTases that synthesize cyclic dipyrimidines for phage resistance, revealing a (R/Q)xW motif dictating pyrimidine selection which suggests a sequential pathway for synthesizing 2’3’-cyclic di-UMP.
ArticleNumber 5078
Author Yang, Chia-Shin
Hou, Mei-Hui
Chen, Yeh
Wang, Yu-Chuan
Ko, Tzu-Ping
Chen, Chao-Jung
Author_xml – sequence: 1
  givenname: Chia-Shin
  surname: Yang
  fullname: Yang, Chia-Shin
  organization: Genomics BioSci & Tech Co. Ltd
– sequence: 2
  givenname: Tzu-Ping
  orcidid: 0000-0003-1794-2638
  surname: Ko
  fullname: Ko, Tzu-Ping
  organization: Institute of Biological Chemistry, Academia Sinica
– sequence: 3
  givenname: Chao-Jung
  orcidid: 0000-0003-3834-9243
  surname: Chen
  fullname: Chen, Chao-Jung
  organization: Graduate Institute of Integrated Medicine, China Medical University, Proteomics Core Laboratory, Department of Medical Research, China Medical University Hospital
– sequence: 4
  givenname: Mei-Hui
  surname: Hou
  fullname: Hou, Mei-Hui
  organization: Genomics BioSci & Tech Co. Ltd
– sequence: 5
  givenname: Yu-Chuan
  orcidid: 0000-0003-2726-9731
  surname: Wang
  fullname: Wang, Yu-Chuan
  organization: Trade Wind Biotech Co. Ltd
– sequence: 6
  givenname: Yeh
  orcidid: 0000-0002-7740-0446
  surname: Chen
  fullname: Chen, Yeh
  email: chyeah6599@nchu.edu.tw
  organization: Department of Food Science and Biotechnology, National Chung Hsing University
BookMark eNp9kk1vFSEUhiemxtbaP-BqEjdusHzNwKxM02pt0sSFH1vCwOGW61y4AmMy_nq5nUatC9nA4bznyXvgPG-OQgzQNC8JfkMwk-eZE94LhClDHAsp0PCkOaGYE0QEZUd_nY-bs5y3uC42EMn5s-aYiR5zSbqTZrlMSy56anNJsylzglYH27o5mOJjqAm_20_e6EOU2-has5gat9aj_ZL8zlsfAOUllDvI_qcPm9ZcX3w6vwrmK5r8N2jDbCaIxdtlKkmH7CDpDPlF89TpKcPZw37afHn_7vPlB3T78frm8uIWmY7IgmgvBoxHMA5zxo2xxBo2OoqBg3AjJ91IrKRDba7DQggYpRa9JoJphhkDdtrcrFwb9Vbtq2WdFhW1V_cXMW2UTsVXj0pao-sL0V47zmXvtMRGj6xnmmgz8APr7craz-MOrIFQO5oeQR9ngr9Tm_hDEcw5ZcNQCa8fCCl-nyEXtfPZwDTpAHHOisqOD70gA63SV_9It3FO9UtWFaGUdX1V0VVlUsw5gfvthmB1mBS1Toqqk6LuJ0UdXLC1KFdx2ED6g_5P1S9tkcQO
CitedBy_id crossref_primary_10_1038_s41467_024_49861_2
Cites_doi 10.1016/j.cell.2012.01.053
10.1038/s41580-020-0244-x
10.1093/nar/gky427
10.1038/s41586-020-2719-5
10.1038/s41467-021-26583-3
10.1016/j.str.2015.01.023
10.1002/pro.3791
10.1038/msb.2011.75
10.1016/j.sbi.2019.08.003
10.1038/34542
10.1107/S2059798319011471
10.1107/S0907444998003254
10.1016/j.jmb.2019.05.042
10.1016/j.tibs.2014.10.008
10.1016/j.cell.2014.07.028
10.1107/S0907444909042589
10.1016/j.cell.2018.06.026
10.1093/nar/gkab165
10.1016/j.cell.2021.09.031
10.1016/j.mib.2021.01.017
10.1093/nar/gkw256
10.1016/j.cell.2020.05.019
10.1101/gr.849004
10.1021/acs.jproteome.8b00644
10.1073/pnas.1801233115
10.1016/j.molcel.2019.12.009
10.1016/j.celrep.2021.109206
10.1107/S0907444911001314
10.1038/s41586-019-1605-5
10.1007/164_2015_35
10.1038/s41467-021-26738-2
10.1038/s41586-019-0953-5
10.1093/nar/gkaa112
10.1038/s41586-022-04716-y
10.1016/j.molcel.2021.10.020
10.3390/molecules25102462
ContentType Journal Article
Copyright The Author(s) 2023
The Author(s) 2023. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Springer Nature Limited 2023
Copyright_xml – notice: The Author(s) 2023
– notice: The Author(s) 2023. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: Springer Nature Limited 2023
DBID C6C
AAYXX
CITATION
3V.
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7T7
7TM
7TO
7X7
7XB
88E
8AO
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
ABUWG
AFKRA
ARAPS
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
C1K
CCPQU
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
H94
HCIFZ
K9.
LK8
M0S
M1P
M7P
P5Z
P62
P64
PIMPY
PQEST
PQQKQ
PQUKI
RC3
SOI
7X8
5PM
DOA
DOI 10.1038/s41467-023-40787-9
DatabaseName SpringerOpen
CrossRef
ProQuest Central (Corporate)
Bacteriology Abstracts (Microbiology B)
Calcium & Calcified Tissue Abstracts
Chemoreception Abstracts
Ecology Abstracts
Entomology Abstracts (Full archive)
Environment Abstracts
Immunology Abstracts
Industrial and Applied Microbiology Abstracts (Microbiology A)
Nucleic Acids Abstracts
Oncogenes and Growth Factors Abstracts
ProQuest Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
ProQuest Pharma Collection
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
ProQuest Central (Alumni)
ProQuest Central
Advanced Technologies & Aerospace Database‎ (1962 - current)
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Technology Collection
ProQuest Natural Science Collection
Environmental Sciences and Pollution Management
ProQuest One Community College
ProQuest Central Korea
Engineering Research Database
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
AIDS and Cancer Research Abstracts
SciTech Premium Collection (Proquest) (PQ_SDU_P3)
ProQuest Health & Medical Complete (Alumni)
Biological Sciences
Health & Medical Collection (Alumni Edition)
PML(ProQuest Medical Library)
Biological Science Database
Advanced Technologies & Aerospace Database
ProQuest Advanced Technologies & Aerospace Collection
Biotechnology and BioEngineering Abstracts
Publicly Available Content Database
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
Genetics Abstracts
Environment Abstracts
MEDLINE - Academic
PubMed Central (Full Participant titles)
Directory of Open Access Journals
DatabaseTitle CrossRef
Publicly Available Content Database
ProQuest Central Student
Oncogenes and Growth Factors Abstracts
ProQuest Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Nucleic Acids Abstracts
SciTech Premium Collection
Environmental Sciences and Pollution Management
Health Research Premium Collection
Natural Science Collection
Biological Science Collection
Chemoreception Abstracts
Industrial and Applied Microbiology Abstracts (Microbiology A)
ProQuest Medical Library (Alumni)
Advanced Technologies & Aerospace Collection
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
ProQuest Technology Collection
Health Research Premium Collection (Alumni)
Biological Science Database
Ecology Abstracts
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
Entomology Abstracts
ProQuest Health & Medical Complete
ProQuest One Academic UKI Edition
Engineering Research Database
ProQuest One Academic
Calcium & Calcified Tissue Abstracts
Technology Collection
Technology Research Database
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central
Genetics Abstracts
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
AIDS and Cancer Research Abstracts
ProQuest SciTech Collection
Advanced Technologies & Aerospace Database
ProQuest Medical Library
Immunology Abstracts
Environment Abstracts
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList CrossRef

MEDLINE - Academic

Publicly Available Content Database
Database_xml – sequence: 1
  dbid: C6C
  name: SpringerOpen
  url: http://www.springeropen.com/
  sourceTypes: Publisher
– sequence: 2
  dbid: DOA
  name: Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 3
  dbid: 8FG
  name: ProQuest Technology Collection
  url: https://search.proquest.com/technologycollection1
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 2041-1723
EndPage 5078
ExternalDocumentID oai_doaj_org_article_8dca18426af4486fa80cab363a1ac94e
10_1038_s41467_023_40787_9
GrantInformation_xml – fundername: Ministry of Science and Technology, Taiwan (Ministry of Science and Technology of Taiwan)
  grantid: 111-2311-B-039-001-MY3
  funderid: https://doi.org/10.13039/501100004663
– fundername: ;
  grantid: 111-2311-B-039-001-MY3
GroupedDBID ---
0R~
39C
3V.
53G
5VS
70F
7X7
88E
8AO
8FE
8FG
8FH
8FI
8FJ
AAHBH
AAJSJ
ABUWG
ACGFO
ACGFS
ACIWK
ACMJI
ACPRK
ACSMW
ADBBV
ADFRT
ADRAZ
AENEX
AFKRA
AFRAH
AHMBA
AJTQC
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AMTXH
AOIJS
ARAPS
ASPBG
AVWKF
AZFZN
BBNVY
BCNDV
BENPR
BGLVJ
BHPHI
BPHCQ
BVXVI
C6C
CCPQU
DIK
EBLON
EBS
EE.
EMOBN
F5P
FEDTE
FYUFA
GROUPED_DOAJ
HCIFZ
HMCUK
HVGLF
HYE
HZ~
KQ8
LGEZI
LK8
LOTEE
M1P
M48
M7P
M~E
NADUK
NAO
NXXTH
O9-
OK1
P2P
P62
PIMPY
PQQKQ
PROAC
PSQYO
RNS
RNT
RNTTT
RPM
SNYQT
SV3
TSG
UKHRP
AAYXX
CITATION
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7T7
7TM
7TO
7XB
8FD
8FK
AZQEC
C1K
DWQXO
FR3
GNUQQ
H94
K9.
P64
PQEST
PQUKI
RC3
SOI
7X8
AFGXO
5PM
ID FETCH-LOGICAL-c518t-267900becf0434ccd1dc3bf20e4e7fb415b1d82903950777eb8a76a173a3033e3
IEDL.DBID RPM
ISSN 2041-1723
IngestDate Fri Oct 04 13:14:33 EDT 2024
Tue Sep 17 21:29:47 EDT 2024
Fri Aug 16 14:00:52 EDT 2024
Thu Oct 10 21:07:22 EDT 2024
Fri Aug 23 02:41:54 EDT 2024
Fri Oct 11 20:46:27 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Language English
License Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c518t-267900becf0434ccd1dc3bf20e4e7fb415b1d82903950777eb8a76a173a3033e3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ORCID 0000-0003-2726-9731
0000-0002-7740-0446
0000-0003-1794-2638
0000-0003-3834-9243
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10442399/
PMID 37604815
PQID 2854122356
PQPubID 546298
PageCount 1
ParticipantIDs doaj_primary_oai_doaj_org_article_8dca18426af4486fa80cab363a1ac94e
pubmedcentral_primary_oai_pubmedcentral_nih_gov_10442399
proquest_miscellaneous_2854967192
proquest_journals_2854122356
crossref_primary_10_1038_s41467_023_40787_9
springer_journals_10_1038_s41467_023_40787_9
PublicationCentury 2000
PublicationDate 2023-08-21
PublicationDateYYYYMMDD 2023-08-21
PublicationDate_xml – month: 08
  year: 2023
  text: 2023-08-21
  day: 21
PublicationDecade 2020
PublicationPlace London
PublicationPlace_xml – name: London
PublicationTitle Nature communications
PublicationTitleAbbrev Nat Commun
PublicationYear 2023
Publisher Nature Publishing Group UK
Nature Publishing Group
Nature Portfolio
Publisher_xml – name: Nature Publishing Group UK
– name: Nature Publishing Group
– name: Nature Portfolio
References Hobbs (CR15) 2022; 605
Sievers (CR35) 2011; 7
Brünger (CR27) 1998; 54
Davies, Bogard, Young, Mekalanos (CR23) 2012; 149
Crooks, Hon, Chandonia, Brenner (CR37) 2004; 14
Govande, Duncan-Lowey, Eaglesham, Whiteley, Kranzusch (CR19) 2021; 35
Ko (CR7) 2022; 13
Steitz (CR17) 1998; 391
Yoon, Waters (CR1) 2021; 60
He, Yin, Galperin, Chou (CR3) 2020; 48
Kranzusch (CR16) 2019; 59
Waterhouse (CR31) 2018; 46
Whiteley (CR12) 2019; 567
CR33
Fatma, Chakravarti, Zeng, Huang (CR14) 2021; 12
Murshudov (CR32) 2011; 67
Zhou (CR4) 2018; 174
Belogurov, Artsimovitch (CR21) 2019; 431
Lowey (CR22) 2020; 182
Trifinopoulos, Nguyen, von Haeseler, Minh (CR36) 2016; 44
Vagin, Teplyakov (CR30) 2010; 66
Duncan-Lowey, McNamara-Bordewick, Tal, Sorek, Kranzusch (CR20) 2021; 81
CR2
Hopfner, Hornung (CR5) 2020; 21
Severin (CR9) 2018; 115
Ko (CR13) 2021; 49
Kato, Ishii, Hirano, Ishitani, Nureki (CR18) 2015; 23
Seifert (CR24) 2015; 40
Marondedze, Wong, Thomas, Irving, Gehring (CR25) 2017; 238
Kranzusch (CR8) 2014; 158
Ye (CR11) 2020; 77
Tal (CR26) 2021; 184
Cohen (CR10) 2019; 574
Chen, Liao, Chang, Lin, Tsai (CR34) 2018; 17
Morehouse (CR6) 2020; 586
Casañal, Lohkamp, Emsley (CR29) 2020; 29
Liebschner (CR28) 2019; 75
AA Govande (40787_CR19) 2021; 35
A Vagin (40787_CR30) 2010; 66
PJ Kranzusch (40787_CR8) 2014; 158
40787_CR2
40787_CR33
J Trifinopoulos (40787_CR36) 2016; 44
GA Belogurov (40787_CR21) 2019; 431
N Tal (40787_CR26) 2021; 184
GB Severin (40787_CR9) 2018; 115
AT Brünger (40787_CR27) 1998; 54
K Kato (40787_CR18) 2015; 23
R Seifert (40787_CR24) 2015; 40
GE Crooks (40787_CR37) 2004; 14
KP Hopfner (40787_CR5) 2020; 21
AT Whiteley (40787_CR12) 2019; 567
BW Davies (40787_CR23) 2012; 149
C Marondedze (40787_CR25) 2017; 238
W Zhou (40787_CR4) 2018; 174
SH Yoon (40787_CR1) 2021; 60
A Casañal (40787_CR29) 2020; 29
S Fatma (40787_CR14) 2021; 12
CJ Chen (40787_CR34) 2018; 17
Q Ye (40787_CR11) 2020; 77
TP Ko (40787_CR7) 2022; 13
TA Steitz (40787_CR17) 1998; 391
A Waterhouse (40787_CR31) 2018; 46
TP Ko (40787_CR13) 2021; 49
PJ Kranzusch (40787_CR16) 2019; 59
B Duncan-Lowey (40787_CR20) 2021; 81
F Sievers (40787_CR35) 2011; 7
B Lowey (40787_CR22) 2020; 182
D Cohen (40787_CR10) 2019; 574
D Liebschner (40787_CR28) 2019; 75
SJ Hobbs (40787_CR15) 2022; 605
BR Morehouse (40787_CR6) 2020; 586
GN Murshudov (40787_CR32) 2011; 67
J He (40787_CR3) 2020; 48
References_xml – volume: 149
  start-page: 358
  year: 2012
  end-page: 370
  ident: CR23
  article-title: Coordinated regulation of accessory genetic elements produces cyclic di-nucleotides for V. cholerae virulence
  publication-title: Cell
  doi: 10.1016/j.cell.2012.01.053
  contributor:
    fullname: Mekalanos
– volume: 21
  start-page: 501
  year: 2020
  end-page: 521
  ident: CR5
  article-title: Molecular mechanisms and cellular functions of cGAS-STING signalling
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/s41580-020-0244-x
  contributor:
    fullname: Hornung
– volume: 46
  start-page: W296
  year: 2018
  end-page: w303
  ident: CR31
  article-title: SWISS-MODEL: homology modelling of protein structures and complexes
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gky427
  contributor:
    fullname: Waterhouse
– volume: 586
  start-page: 429
  year: 2020
  end-page: 433
  ident: CR6
  article-title: STING cyclic dinucleotide sensing originated in bacteria
  publication-title: Nature
  doi: 10.1038/s41586-020-2719-5
  contributor:
    fullname: Morehouse
– volume: 13
  year: 2022
  ident: CR7
  article-title: Crystal structure and functional implication of bacterial STING
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-021-26583-3
  contributor:
    fullname: Ko
– ident: CR2
– volume: 23
  start-page: 843
  year: 2015
  end-page: 850
  ident: CR18
  article-title: Structural basis for the catalytic mechanism of DncV, bacterial homolog of cyclic GMP-AMP synthase
  publication-title: Structure
  doi: 10.1016/j.str.2015.01.023
  contributor:
    fullname: Nureki
– volume: 29
  start-page: 1069
  year: 2020
  end-page: 1078
  ident: CR29
  article-title: Current developments in Coot for macromolecular model building of Electron Cryo-microscopy and Crystallographic Data
  publication-title: Protein Sci.
  doi: 10.1002/pro.3791
  contributor:
    fullname: Emsley
– volume: 7
  start-page: 539
  year: 2011
  ident: CR35
  article-title: Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
  publication-title: Mol. Syst. Biol.
  doi: 10.1038/msb.2011.75
  contributor:
    fullname: Sievers
– ident: CR33
– volume: 59
  start-page: 178
  year: 2019
  end-page: 187
  ident: CR16
  article-title: cGAS and CD-NTase enzymes: structure, mechanism, and evolution
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2019.08.003
  contributor:
    fullname: Kranzusch
– volume: 391
  start-page: 231
  year: 1998
  end-page: 232
  ident: CR17
  article-title: A mechanism for all polymerases
  publication-title: Nature
  doi: 10.1038/34542
  contributor:
    fullname: Steitz
– volume: 75
  start-page: 861
  year: 2019
  end-page: 877
  ident: CR28
  article-title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix
  publication-title: Acta Crystallogr. D. Struct. Biol.
  doi: 10.1107/S2059798319011471
  contributor:
    fullname: Liebschner
– volume: 54
  start-page: 905
  year: 1998
  end-page: 921
  ident: CR27
  article-title: Crystallography & NMR system: A new software suite for macromolecular structure determination
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444998003254
  contributor:
    fullname: Brünger
– volume: 431
  start-page: 3975
  year: 2019
  end-page: 4006
  ident: CR21
  article-title: The mechanisms of substrate selection, catalysis, and translocation by the elongating RNA polymerase
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2019.05.042
  contributor:
    fullname: Artsimovitch
– volume: 40
  start-page: 8
  year: 2015
  end-page: 15
  ident: CR24
  article-title: cCMP and cUMP: emerging second messengers
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2014.10.008
  contributor:
    fullname: Seifert
– volume: 158
  start-page: 1011
  year: 2014
  end-page: 1021
  ident: CR8
  article-title: Structure-guided reprogramming of human cGAS dinucleotide linkage specificity
  publication-title: Cell
  doi: 10.1016/j.cell.2014.07.028
  contributor:
    fullname: Kranzusch
– volume: 66
  start-page: 22
  year: 2010
  end-page: 25
  ident: CR30
  article-title: Molecular replacement with MOLREP
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444909042589
  contributor:
    fullname: Teplyakov
– volume: 174
  start-page: 300
  year: 2018
  end-page: 311.e311
  ident: CR4
  article-title: Structure of the human cGAS-DNA complex reveals enhanced control of immune surveillance
  publication-title: Cell
  doi: 10.1016/j.cell.2018.06.026
  contributor:
    fullname: Zhou
– volume: 49
  start-page: 4725
  year: 2021
  end-page: 4737
  ident: CR13
  article-title: Crystal structure and functional implication of a bacterial cyclic AMP-AMP-GMP synthetase
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkab165
  contributor:
    fullname: Ko
– volume: 184
  start-page: 5728
  year: 2021
  end-page: 5739.e5716
  ident: CR26
  article-title: Cyclic CMP and cyclic UMP mediate bacterial immunity against phages
  publication-title: Cell
  doi: 10.1016/j.cell.2021.09.031
  contributor:
    fullname: Tal
– volume: 60
  start-page: 96
  year: 2021
  end-page: 103
  ident: CR1
  article-title: The ever-expanding world of bacterial cyclic oligonucleotide second messengers
  publication-title: Curr. Opin. Microbiol.
  doi: 10.1016/j.mib.2021.01.017
  contributor:
    fullname: Waters
– volume: 44
  start-page: W232
  year: 2016
  end-page: 235
  ident: CR36
  article-title: W-IQ-TREE: a fast online phylogenetic tool for maximum likelihood analysis
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkw256
  contributor:
    fullname: Minh
– volume: 182
  start-page: 38
  year: 2020
  end-page: 49.e17
  ident: CR22
  article-title: CBASS immunity uses CARF-related effectors to sense 3’-5’- and 2’-5’-linked cyclic oligonucleotide signals and protect bacteria from phage infection
  publication-title: Cell
  doi: 10.1016/j.cell.2020.05.019
  contributor:
    fullname: Lowey
– volume: 14
  start-page: 1188
  year: 2004
  end-page: 1190
  ident: CR37
  article-title: WebLogo: a sequence logo generator
  publication-title: Genome Res.
  doi: 10.1101/gr.849004
  contributor:
    fullname: Brenner
– volume: 17
  start-page: 3997
  year: 2018
  end-page: 4007
  ident: CR34
  article-title: Identification of urinary metabolite biomarkers of type 2 diabetes nephropathy using an untargeted metabolomic approach
  publication-title: J. Proteome Res.
  doi: 10.1021/acs.jproteome.8b00644
  contributor:
    fullname: Tsai
– volume: 115
  start-page: E6048
  year: 2018
  end-page: e6055
  ident: CR9
  article-title: Direct activation of a phospholipase by cyclic GMP-AMP in El Tor Vibrio cholerae
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1801233115
  contributor:
    fullname: Severin
– volume: 77
  start-page: 709
  year: 2020
  end-page: 722.e707
  ident: CR11
  article-title: HORMA domain proteins and a Trip13-like ATPase regulate bacterial cGAS-like enzymes to mediate bacteriophage iImmunity
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2019.12.009
  contributor:
    fullname: Ye
– volume: 35
  start-page: 109206
  year: 2021
  ident: CR19
  article-title: Molecular basis of CD-NTase nucleotide selection in CBASS anti-phage defense
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2021.109206
  contributor:
    fullname: Kranzusch
– volume: 67
  start-page: 355
  year: 2011
  end-page: 367
  ident: CR32
  article-title: REFMAC5 for the refinement of macromolecular crystal structures
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444911001314
  contributor:
    fullname: Murshudov
– volume: 574
  start-page: 691
  year: 2019
  end-page: 695
  ident: CR10
  article-title: Cyclic GMP-AMP signalling protects bacteria against viral infection
  publication-title: Nature
  doi: 10.1038/s41586-019-1605-5
  contributor:
    fullname: Cohen
– volume: 238
  start-page: 87
  year: 2017
  end-page: 103
  ident: CR25
  article-title: Cyclic nucleotide monophosphates in plants and plant signaling
  publication-title: Handb. Exp. Pharm.
  doi: 10.1007/164_2015_35
  contributor:
    fullname: Gehring
– volume: 12
  year: 2021
  ident: CR14
  article-title: Molecular mechanisms of the CdnG-Cap5 antiphage defense system employing 3’,2’-cGAMP as the second messenger
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-021-26738-2
  contributor:
    fullname: Huang
– volume: 567
  start-page: 194
  year: 2019
  end-page: 199
  ident: CR12
  article-title: Bacterial cGAS-like enzymes synthesize diverse nucleotide signals
  publication-title: Nature
  doi: 10.1038/s41586-019-0953-5
  contributor:
    fullname: Whiteley
– volume: 48
  start-page: 2807
  year: 2020
  end-page: 2829
  ident: CR3
  article-title: Cyclic di-AMP, a second messenger of primary importance: tertiary structures and binding mechanisms
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkaa112
  contributor:
    fullname: Chou
– volume: 605
  start-page: 522
  year: 2022
  end-page: 526
  ident: CR15
  article-title: Phage anti-CBASS and anti-Pycsar nucleases subvert bacterial immunity
  publication-title: Nature
  doi: 10.1038/s41586-022-04716-y
  contributor:
    fullname: Hobbs
– volume: 81
  start-page: 5039
  year: 2021
  end-page: 5051.e5035
  ident: CR20
  article-title: Effector-mediated membrane disruption controls cell death in CBASS antiphage defense
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2021.10.020
  contributor:
    fullname: Kranzusch
– volume: 77
  start-page: 709
  year: 2020
  ident: 40787_CR11
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2019.12.009
  contributor:
    fullname: Q Ye
– volume: 567
  start-page: 194
  year: 2019
  ident: 40787_CR12
  publication-title: Nature
  doi: 10.1038/s41586-019-0953-5
  contributor:
    fullname: AT Whiteley
– volume: 35
  start-page: 109206
  year: 2021
  ident: 40787_CR19
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2021.109206
  contributor:
    fullname: AA Govande
– volume: 158
  start-page: 1011
  year: 2014
  ident: 40787_CR8
  publication-title: Cell
  doi: 10.1016/j.cell.2014.07.028
  contributor:
    fullname: PJ Kranzusch
– volume: 49
  start-page: 4725
  year: 2021
  ident: 40787_CR13
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkab165
  contributor:
    fullname: TP Ko
– volume: 574
  start-page: 691
  year: 2019
  ident: 40787_CR10
  publication-title: Nature
  doi: 10.1038/s41586-019-1605-5
  contributor:
    fullname: D Cohen
– volume: 391
  start-page: 231
  year: 1998
  ident: 40787_CR17
  publication-title: Nature
  doi: 10.1038/34542
  contributor:
    fullname: TA Steitz
– volume: 149
  start-page: 358
  year: 2012
  ident: 40787_CR23
  publication-title: Cell
  doi: 10.1016/j.cell.2012.01.053
  contributor:
    fullname: BW Davies
– volume: 29
  start-page: 1069
  year: 2020
  ident: 40787_CR29
  publication-title: Protein Sci.
  doi: 10.1002/pro.3791
  contributor:
    fullname: A Casañal
– volume: 46
  start-page: W296
  year: 2018
  ident: 40787_CR31
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gky427
  contributor:
    fullname: A Waterhouse
– volume: 21
  start-page: 501
  year: 2020
  ident: 40787_CR5
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/s41580-020-0244-x
  contributor:
    fullname: KP Hopfner
– volume: 40
  start-page: 8
  year: 2015
  ident: 40787_CR24
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2014.10.008
  contributor:
    fullname: R Seifert
– volume: 174
  start-page: 300
  year: 2018
  ident: 40787_CR4
  publication-title: Cell
  doi: 10.1016/j.cell.2018.06.026
  contributor:
    fullname: W Zhou
– volume: 44
  start-page: W232
  year: 2016
  ident: 40787_CR36
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkw256
  contributor:
    fullname: J Trifinopoulos
– volume: 48
  start-page: 2807
  year: 2020
  ident: 40787_CR3
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkaa112
  contributor:
    fullname: J He
– volume: 12
  year: 2021
  ident: 40787_CR14
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-021-26738-2
  contributor:
    fullname: S Fatma
– volume: 182
  start-page: 38
  year: 2020
  ident: 40787_CR22
  publication-title: Cell
  doi: 10.1016/j.cell.2020.05.019
  contributor:
    fullname: B Lowey
– volume: 184
  start-page: 5728
  year: 2021
  ident: 40787_CR26
  publication-title: Cell
  doi: 10.1016/j.cell.2021.09.031
  contributor:
    fullname: N Tal
– volume: 7
  start-page: 539
  year: 2011
  ident: 40787_CR35
  publication-title: Mol. Syst. Biol.
  doi: 10.1038/msb.2011.75
  contributor:
    fullname: F Sievers
– volume: 23
  start-page: 843
  year: 2015
  ident: 40787_CR18
  publication-title: Structure
  doi: 10.1016/j.str.2015.01.023
  contributor:
    fullname: K Kato
– volume: 17
  start-page: 3997
  year: 2018
  ident: 40787_CR34
  publication-title: J. Proteome Res.
  doi: 10.1021/acs.jproteome.8b00644
  contributor:
    fullname: CJ Chen
– volume: 586
  start-page: 429
  year: 2020
  ident: 40787_CR6
  publication-title: Nature
  doi: 10.1038/s41586-020-2719-5
  contributor:
    fullname: BR Morehouse
– volume: 54
  start-page: 905
  year: 1998
  ident: 40787_CR27
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444998003254
  contributor:
    fullname: AT Brünger
– volume: 66
  start-page: 22
  year: 2010
  ident: 40787_CR30
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444909042589
  contributor:
    fullname: A Vagin
– volume: 75
  start-page: 861
  year: 2019
  ident: 40787_CR28
  publication-title: Acta Crystallogr. D. Struct. Biol.
  doi: 10.1107/S2059798319011471
  contributor:
    fullname: D Liebschner
– volume: 431
  start-page: 3975
  year: 2019
  ident: 40787_CR21
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2019.05.042
  contributor:
    fullname: GA Belogurov
– volume: 13
  year: 2022
  ident: 40787_CR7
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-021-26583-3
  contributor:
    fullname: TP Ko
– volume: 81
  start-page: 5039
  year: 2021
  ident: 40787_CR20
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2021.10.020
  contributor:
    fullname: B Duncan-Lowey
– ident: 40787_CR33
– volume: 115
  start-page: E6048
  year: 2018
  ident: 40787_CR9
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1801233115
  contributor:
    fullname: GB Severin
– volume: 605
  start-page: 522
  year: 2022
  ident: 40787_CR15
  publication-title: Nature
  doi: 10.1038/s41586-022-04716-y
  contributor:
    fullname: SJ Hobbs
– volume: 238
  start-page: 87
  year: 2017
  ident: 40787_CR25
  publication-title: Handb. Exp. Pharm.
  doi: 10.1007/164_2015_35
  contributor:
    fullname: C Marondedze
– volume: 60
  start-page: 96
  year: 2021
  ident: 40787_CR1
  publication-title: Curr. Opin. Microbiol.
  doi: 10.1016/j.mib.2021.01.017
  contributor:
    fullname: SH Yoon
– volume: 59
  start-page: 178
  year: 2019
  ident: 40787_CR16
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2019.08.003
  contributor:
    fullname: PJ Kranzusch
– volume: 67
  start-page: 355
  year: 2011
  ident: 40787_CR32
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444911001314
  contributor:
    fullname: GN Murshudov
– volume: 14
  start-page: 1188
  year: 2004
  ident: 40787_CR37
  publication-title: Genome Res.
  doi: 10.1101/gr.849004
  contributor:
    fullname: GE Crooks
– ident: 40787_CR2
  doi: 10.3390/molecules25102462
SSID ssj0000391844
Score 2.476579
Snippet Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria; however,...
Abstract Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria;...
Abstract Purine-containing nucleotide second messengers regulate diverse cellular activities. Cyclic di-pyrimidines mediate anti-phage functions in bacteria;...
SourceID doaj
pubmedcentral
proquest
crossref
springer
SourceType Open Website
Open Access Repository
Aggregation Database
Publisher
StartPage 5078
SubjectTerms 140/58
631/326/41/2536
631/45/607
631/535/1266
Bacteria
Crystal structure
Cytosine
Humanities and Social Sciences
multidisciplinary
Nucleotides
Phages
Proteins
Pyrimidines
Science
Science (multidisciplinary)
Second messengers
Structural analysis
Structure-function relationships
Substrates
Synthesis
Uracil
SummonAdditionalLinks – databaseName: Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELZQJSQuiKcIFGQkbmCtHTu2cyyFUnHgAkW9WX5FRKyy1WZ7CL-esZ0tm0qIC8cklvyY8XyfM-MZhN6oVnseakkEwBURjHHSUheI4l5y3jKtQw6Q_SLPL8Tny-byoNRXigkr6YHLwq108BZOIbW0HZwkZGc19dZxyS2zvhUxW1_WHBymsg1O3Qgx35KhXK9GkW0CQBRJritF2gUS5YT9C5Z5O0bylqM048_ZA3R_Jo74pAz4IboTh0fobiklOT1G0-l2AqK3xiUh7PU2YjsEnGCr_O3D_UHsON502E8ennHoydWUansBiEUyTgMwwrH_BWPA_tPJ19WHwX8n6_5nxENKfbzZ9WFa7zLdjVuAwPEJujj7-O30nMxlFYhvmN6RWqqWUpBdRwUX3gcWPHddTaOIqnOA6I6F5F_lLZBFpaLTVknLFLeAdzzyp-ho2AzxGcLONY7ayLn0wKu419b5WNfWdUDLWHQVertfYnNVsmeY7PXm2hSBGBCIyQIxbYXeJynctEyZr_ML0Acz64P5lz5U6HgvQzNvx9Gka6IMiFAjK_T65jNspOQdsUPcXJc2rVTAeCukF7JfDGj5Zeh_5JTccKhNmRRhCu_2avKn97_P-Pn_mPELdK9Oak3B5LFjdARqFl8CU9q5V3lT_AZVXhM8
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: ProQuest Technology Collection
  dbid: 8FG
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3LbtQwFLWgCIkNojxEoEVGYgfWxLHHdlaoLZ1WLNhAUXeWX4Goo2SYTBfp1_fayUxJJVjmIcXJsX1O7rXPReiDLJVjvhCEA10RTikjZW49kcwJxkqqlE8LZL-J8wv-9XJ-OQbcunFZ5XZOTBO1b12Mkc_iTj8KXDYXn1d_SKwaFbOrYwmNh-gRjU54caf44mwXY4nu54rzca9MztSs42lmAKIiMYElSTnho2TbP9Ga91dK3kuXJhZaPENPR_mIjwa899GD0DxHj4eCkv0L1J-se5B7SzzYwl6vAzaNx5G8hpgfrv9aQY7bCrvewTH2NVn1scIXUFkgXd-ALuzqG2gDdmdH32dfGveTLOurgJtogNxuat8vN0n0hjUQYfcSXSxOf5yck7G4AnFzqjakELLMc0CwyjnjznnqHbNVkQceZGWB1y31McvKSpCMUgarjBSGSmaA9Vhgr9Be0zbhNcLWzm1uAmPCgbpiThnrQlEYW4E4o8Fm6OP2E-vV4KGhU-6bKT0AogEQnQDRZYaOIwq7O6P_dTrRrn_pcThp5Z0BaAthKvi_FJVRuTOWCWaocSUPGTrYYqjHQdnpuy6Uofe7yzCcYo7ENKG9Hu4phQTdmyE1wX7SoOmVpv6djLnh1zb6KcIrfNp2k7un__uN3_y_sW_Rk1jjPgayC3qA9qADhUNQQhv7LnX3W9bpCes
  priority: 102
  providerName: ProQuest
– databaseName: Scholars Portal Open Access Journals
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Nb9QwELVKERIXxKcIFGQkbmAax17bOSBUCqVCggss6s3yVyBilZRkKxF-PWMnKaQqN45JHCX2m8l7ztgzCD2VpXLMF4JwoCvCKWWkzK0nkjnBWEmV8mmB7EdxvObvT1YnO2gudzQNYH_p1C7Wk1p3mxc_fwyvwOFfjlvG1X7Pk7sD-5AYlZKkvIKuFpzxaPEfJrmfvszx4ZxPe2cuv3XBTymN_0J7Xlw5eSF8mljp6Ca6MclJfDDifwvthOY2ujYWmBzuoOGwG0D-bfCYJvasC9g0HkcyG_8B4vqvFeW4rbAbHBxjX5PTIVb8AmoLpB8a0Il9_QveAbt3B5_23zTuC9nU3wNuYkLkdlv7YbNNIjh0QIz9XbQ-evv58JhMxRaIW1G1JYWQZZ4DolUOI-ecp94xWxV54EFWFnjeUh-jrqwECSllsMpIYahkBliQBXYP7TZtE-4jbO3K5iYwJhyoLeaUsS4UhbEViDUabIaezUOsT8ecGjrFwpnSIyAaANEJEF1m6HVE4bxlzIedTrTdVz25l1beGYC2EKaC-aaojMqdsUwwQ40recjQ3oyhnm1Mx82jFOTRSmToyfllcK8YMzFNaM_GNqWQoIMzpBbYL15oeaWpv6VE3TDVjfkVoQvPZzP58_R_9_jB_-jxQ3S9iGadw4eQ7qFdMLPwCPTT1j5OTvEbEJ4alw
  priority: 102
  providerName: Scholars Portal
– databaseName: SpringerOpen
  dbid: C6C
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Nb9QwFLSgCIkLonyItKVyJW5gNY4d2zmWhVL1wAWKerP8FRGx8lab7SH8-j472YVUcOCY2FHizLNm7GePEXorG-WYrwThQFeEU8pIU1pPJHOCsYYq5fMC2S_i4opfXtfXk01O2gszy98zddrz3JWBWUjKOEnSPESPairKFMELsdjNpySnc8X5tC_m74_OuCdb9M905f1VkfdSo5lxzp-hp5NUxGcjtvvoQYjP0ePx8MjhBRoW6wGk3RKPFrC364BN9DgR1Ti_h7s_VovjVYvd4OAa-47cDOk0L6CtQPohggbsu1_wDdh9Pvt6-jG672TZ_Qw4JrPj1abzw3KTBW5YA-n1L9HV-adviwsyHaRAXE3VhlRCNmUJaLUlZ9w5T71jtq3KwINsLXC4pT5lVFkD8lDKYJWRwlDJDDAcC-wV2ourGF4jbG1tSxMYEw6UFHPKWBeqytgWhBgNtkDvtr9Y34x-GTrnuZnSIyAaANEZEN0U6ENCYVczeV3nGxACeuo6WnlnANpKmBbGkqI1qnTGMsEMNa7hoUBHWwz11AF7nTaGUpA-tSjQya4Yuk7Kh5gYVrdjnUZI0LgFUjPsZx80L4ndj2zCDcPY5J0ITXi_DZPfb_93iw_-r_ohepLOt0-T2BU9QnsQUOENqKCNPc7hfwfPWALr
  priority: 102
  providerName: Springer Nature
Title Crystal structure and functional implications of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases
URI https://link.springer.com/article/10.1038/s41467-023-40787-9
https://www.proquest.com/docview/2854122356
https://search.proquest.com/docview/2854967192
https://pubmed.ncbi.nlm.nih.gov/PMC10442399
https://doaj.org/article/8dca18426af4486fa80cab363a1ac94e
Volume 14
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Pb9MwFLa2ISQuiJ8iMCojcQOvcezazrEr66ZKmybGUG-R7TgQ0SVV0x3CX8-z04xlEhcuifJDspP37O-z3_NnhD7KVFmWJ4JwgCvCKWUkjU1OJLOCsZQqlYcE2Qtxds0Xy8lyD4l-LUxI2remPKpWN0dV-TPkVq5v7LjPExtfns9gCOF169LxPtqXjN0bo4f-1xfB-W6FTMzUuOGhPwB4Ij5sJYnXCvXZIF6pZABIQbd_QDYfpko-iJcGGJo_Q093_BFPu3o-R3uueoEedztKti9RO9u0wPdWuNOFvd04rKsce_TqJv1weS-FHNcFtq2Fa5yXZN36Lb4Ayxxp2gqIYVP-hjpgezq9Gn-p7HeyKn85XHkF5Hpb5u1qG1iv2wASNq_Q9fzk2-yM7HZXIHZC1ZYkQqZxDCYsYs64tTnNLTNFEjvuZGEA2A3NfZiVpcAZpXRGaSk0lUwD7DHHXqODqq7cG4SNmZhYO8aEBXrFrNLGuiTRpgB2Rp2J0Kf-F2frTkQjC8FvprLONhnYJgu2ydIIHXsr3L3pBbDDjXrzI9u5QaZyq8HKidAFDDBFoVVstWGCaaptyl2EDnsbZrtW2WR-tSgFPjQREfpw9xjakw-S6MrVt907qZBAfCOkBrYfVGj4BBw1KHP3jhmhz72b_C3931_89v9LeoeeJN6vY-jv6CE6AOdy74Embc0I2sZSwlHNT0fo0XS6uFrA-fjk4vIr3J2J2ShMQMDxnKtRaEN_AMCHGuw
link.rule.ids 230,315,733,786,790,870,891,2115,12083,12792,21416,24346,27955,27956,31752,31753,33406,33407,33777,33778,41153,42222,43343,43633,43838,51609,53825,53827,74100,74390,74657
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1db9MwFLWgE4IXxKfIGGAk3sBqHLu284S2sVFgVAg2tDfLX4FoVVKa7iH8eq6TtKOT4DGJpTg5ts_Jvc65CL2SuXLMZ4JwoCvCKWUkT60nkjnBWE6V8t0G2ZmYnvGP55PzIeDWDNsq12tit1D72sUY-Tj-6UeByybi7eIXiVWjYnZ1KKFxE-1Ey001QjsHR7MvXzdRluh_rjgf_pZJmRo3vFsbgKpITGFJkm8xUmfcv6U2r--VvJYw7Xjo-B66OwhIvN8jfh_dCNUDdKsvKdk-RO3hsgXBN8e9MezlMmBTeRzpq4_64fKvPeS4LrBrHRxjX5JFG2t8AZkF0rQVKMOm_A19wO79_rfxu8p9J_PyIuAqWiDXq9K381Une8MSqLB5hM6Oj04Pp2Qor0DchKoVyYTM0xQwLFLOuHOeesdskaWBB1lYYHZLfcyzshxEo5TBKiOFoZIZ4D0W2GM0quoqPEHY2olNTWBMONBXzCljXcgyYwuQZzTYBL1ev2K96F00dJf9Zkr3gGgARHeA6DxBBxGFTcvogN2dqJc_9DChtPLOALSZMAV8YYrCqNQZywQz1LichwTtrTHUw7Rs9NUgStDLzWWYUDFLYqpQX_ZtciFB-SZIbWG_1aHtK1X5s7Pmho_b6KgIj_BmPUyu7v7vJ979f2dfoNvT088n-uTD7NNTdCdWvI9h7YzuoREMpvAMdNHKPh8G_x_8hQ5C
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELagCMSl4qmGFjASN7A2jr22c0KlZVseqpCgqDfLr0DEKlk220P49Yyd7JatBMckluLkG_v77BnPIPRSlsoxXwjCga4Ip5SRMreeSOYEYyVVyqcA2TNxes4_XEwvxvinbgyrXM-JaaL2rYt75JN40o8Cl03FpBrDIj4fz94sfpFYQSp6WsdyGjfRrSiyYxkHNTvZ7LfETOiK8_HcTM7UpONplgDSItGZJUm5xU0phf-W7rweNXnNdZoYaXYP7Y5SEh8O2N9HN0LzAN0eikv2D1F_tOxB-s3xkCL2chmwaTyORDbs_-H6r2hy3FbY9Q6usa_Joo_VvoDWAun6BjRiV_-GPmB3cvhlcty4b2Re_wy4icmQ21Xt-_kqCeCwBFLsHqHz2buvR6dkLLRA3JSqFSmELPMc0KxyzrhznnrHbFXkgQdZWeB4S330uLIS5KOUwSojhaGSGWBAFthjtNO0TdhD2NqpzU1gTDhQWswpY10oCmMrEGo02Ay9Wv9ivRjyaejkB2dKD4BoAEQnQHSZobcRhU3LmAs73WiX3_U4tLTyzgC0hTAVrDVFZVTujGWCGWpcyUOGDtYY6nGAdvrKnDL0YvMYhlb0l5gmtJdDm1JI0MAZUlvYb3Vo-0lT_0hJumGZG3Mrwie8XpvJ1dv__cVP_t_Z5-gOWL3-9P7s4z66W0TbzWGmowdoB2wpPAWBtLLPkuX_AeIZEQg
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Crystal+structure+and+functional+implications+of+cyclic+di-pyrimidine-synthesizing+cGAS%2FDncV-like+nucleotidyltransferases&rft.jtitle=Nature+communications&rft.au=Chia-Shin+Yang&rft.au=Tzu-Ping+Ko&rft.au=Chao-Jung+Chen&rft.au=Mei-Hui+Hou&rft.date=2023-08-21&rft.pub=Nature+Portfolio&rft.eissn=2041-1723&rft.volume=14&rft.issue=1&rft.spage=1&rft.epage=14&rft_id=info:doi/10.1038%2Fs41467-023-40787-9&rft.externalDBID=DOA&rft.externalDocID=oai_doaj_org_article_8dca18426af4486fa80cab363a1ac94e
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2041-1723&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2041-1723&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2041-1723&client=summon