The crystal structure of bromide-bound GtACR1 reveals a pre-activated state in the transmembrane anion tunnel

The crystal structure of the light-gated anion channel GtACR1 reported in our previous Research Article (Li et al., 2019) revealed a continuous tunnel traversing the protein from extracellular to intracellular pores. We proposed the tunnel as the conductance channel closed by three constrictions: C1...

Full description

Saved in:
Bibliographic Details
Published ineLife Vol. 10
Main Authors Li, Hai, Huang, Chia-Ying, Govorunova, Elena G, Sineshchekov, Oleg A, Yi, Adrian, Rothschild, Kenneth J, Wang, Meitian, Zheng, Lei, Spudich, John L
Format Journal Article
LanguageEnglish
Published Cambridge eLife Science Publications, Ltd 17.05.2021
eLife Sciences Publications Ltd
eLife Sciences Publications, Ltd
Subjects
ACR
Binding sites
bromide binding
Channel opening
Channel pores
channelrhodopsin
Chloride
Crystal structure
Crystals
Data collection
Free energy
GtACR1
Guillardia theta
optogenetics
Proteins
Research Advance
Structural Biology and Molecular Biophysics
Structure
Canada
Online AccessGet full text

Cover

Abstract The crystal structure of the light-gated anion channel GtACR1 reported in our previous Research Article (Li et al., 2019) revealed a continuous tunnel traversing the protein from extracellular to intracellular pores. We proposed the tunnel as the conductance channel closed by three constrictions: C1 in the extracellular half, mid-membrane C2 containing the photoactive site, and C3 on the cytoplasmic side. Reported here, the crystal structure of bromide-bound GtACR1 reveals structural changes that relax the C1 and C3 constrictions, including a novel salt-bridge switch mechanism involving C1 and the photoactive site. These findings indicate that substrate binding induces a transition from an inactivated state to a pre-activated state in the dark that facilitates channel opening by reducing free energy in the tunnel constrictions. The results provide direct evidence that the tunnel is the closed form of the channel of GtACR1 and shed light on the light-gated channel activation mechanism.
AbstractList The crystal structure of the light-gated anion channel GtACR1 reported in our previous Research Article (Li et al., 2019) revealed a continuous tunnel traversing the protein from extracellular to intracellular pores. We proposed the tunnel as the conductance channel closed by three constrictions: C1 in the extracellular half, mid-membrane C2 containing the photoactive site, and C3 on the cytoplasmic side. Reported here, the crystal structure of bromide-bound GtACR1 reveals structural changes that relax the C1 and C3 constrictions, including a novel salt-bridge switch mechanism involving C1 and the photoactive site. These findings indicate that substrate binding induces a transition from an inactivated state to a pre-activated state in the dark that facilitates channel opening by reducing free energy in the tunnel constrictions. The results provide direct evidence that the tunnel is the closed form of the channel of GtACR1 and shed light on the light-gated channel activation mechanism.
The crystal structure of the light-gated anion channel Gt ACR1 reported in our previous Research Article (Li et al., 2019) revealed a continuous tunnel traversing the protein from extracellular to intracellular pores. We proposed the tunnel as the conductance channel closed by three constrictions: C1 in the extracellular half, mid-membrane C2 containing the photoactive site, and C3 on the cytoplasmic side. Reported here, the crystal structure of bromide-bound Gt ACR1 reveals structural changes that relax the C1 and C3 constrictions, including a novel salt-bridge switch mechanism involving C1 and the photoactive site. These findings indicate that substrate binding induces a transition from an inactivated state to a pre-activated state in the dark that facilitates channel opening by reducing free energy in the tunnel constrictions. The results provide direct evidence that the tunnel is the closed form of the channel of Gt ACR1 and shed light on the light-gated channel activation mechanism.
Audience Academic
Author Govorunova, Elena G
Rothschild, Kenneth J
Wang, Meitian
Sineshchekov, Oleg A
Li, Hai
Yi, Adrian
Zheng, Lei
Huang, Chia-Ying
Spudich, John L
Author_xml – sequence: 1
  fullname: Li, Hai
– sequence: 2
  fullname: Huang, Chia-Ying
– sequence: 3
  fullname: Govorunova, Elena G
– sequence: 4
  fullname: Sineshchekov, Oleg A
– sequence: 5
  fullname: Yi, Adrian
– sequence: 6
  fullname: Rothschild, Kenneth J
– sequence: 7
  fullname: Wang, Meitian
– sequence: 8
  fullname: Zheng, Lei
– sequence: 9
  fullname: Spudich, John L
BookMark eNptkt9rFDEQxxep2Fr75D-w4ItF7szvzb4Ix6H14ECoFXwL2WT2mmM3qUn2sP-9ubuinpg8TJh8vt9hhnlZnfngoapeYzRvOGfvYe16mAveIvqsuiCIoxmS7PvZX-_z6iqlLSqnYVLi9kV1TmnbSsblRTXe3UNt4mPKeqhTjpPJU4Q69HUXw-gszLoweVvf5MXyFtcRdqCHVOv6IcJMm-x2OoMtyhJq5-tc7HLUPo0wdiVCrb0LJT95D8Or6nlf5HD1FC-rb58-3i0_z9ZfblbLxXpmhMB5ZpmwxpimbQUHoglmqKOS8gZboAZzCqZruGEG6Y4SKyyltJd9R7gwtBOUXlaro68Neqseoht1fFRBO3VIhLhROmZnBlAEyVIIesCcMGJQx6xpO8ybhgshzd7rw9HrYepGsAZ86W84MT398e5ebcJOSdwQwlAxePtkEMOPCVJWo0sGhqFMJ0xJEU4kKx00e_TNP-g2TNGXURWq5QQRKcgfaqNLA873odQ1e1O1EIJKJluJCzX_D1WuhdGZskW9K_kTwfWJoDAZfuaNnlJSq6-3p-y7I2tiSClC_3seGKn9YqrDYqrDYtJfC4zU1Q
CitedBy_id crossref_primary_10_3389_fchem_2022_879609
crossref_primary_10_1128_mbio_03039_22
crossref_primary_10_1093_femsyr_foac047
crossref_primary_10_7554_eLife_72264
crossref_primary_10_1073_pnas_2117433119
crossref_primary_10_1016_j_jbc_2023_105305
crossref_primary_10_1007_s12551_023_01046_9
crossref_primary_10_3389_fncel_2021_800313
Cites_doi 10.1016/j.bpj.2019.10.009
10.1021/ja00244a038
10.1021/j100288a011
10.1107/S0907444909047374
10.1107/S1600577518016570
10.1073/pnas.1513602112
10.1107/S0907444909047337
10.1107/S1399004715005210
10.1107/S2059798320006348
10.1021/ar300087y
10.1107/S0907444909052925
10.1107/S0021889807021206
10.1562/0031-8655(2002)076<0341:AFTISO>2.0.CO;2
10.1016/j.str.2004.02.015
10.1038/s41586-018-0511-6
10.1073/pnas.1525269113
10.1107/S1600577517014503
10.1074/jbc.M303719200
10.1107/S2059798315021683
10.1038/s42003-018-0123-6
10.1371/journal.pcbi.1002708
10.1107/S0907444904019158
10.1021/acs.biochem.7b00002
10.1021/acs.biochem.6b00104
10.1126/science.aaa7484
10.7554/eLife.41741
10.1038/ncomms12677
10.1021/bi0361968
ContentType Journal Article
Copyright COPYRIGHT 2021 eLife Science Publications, Ltd.
2021, Li et al. This work is published under https://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.
2021, Li et al 2021 Li et al
Copyright_xml – notice: COPYRIGHT 2021 eLife Science Publications, Ltd.
– notice: 2021, Li et al. This work is published under https://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: 2021, Li et al 2021 Li et al
DBID AAYXX
CITATION
ISR
3V.
7X7
7XB
88E
88I
8FE
8FH
8FI
8FJ
8FK
ABUWG
AFKRA
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
FYUFA
GHDGH
GNUQQ
HCIFZ
K9.
LK8
M0S
M1P
M2P
M7P
PIMPY
PQEST
PQQKQ
PQUKI
PRINS
Q9U
7X8
5PM
DOA
DOI 10.7554/eLife.65903
DatabaseName CrossRef
Gale In Context: Science
ProQuest Central (Corporate)
Health & Medical Collection (Proquest)
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
Science Database (Alumni Edition)
ProQuest SciTech 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
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Natural Science Collection
ProQuest One Community College
ProQuest Central
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
ProQuest Biological Science Collection
Health & Medical Collection (Alumni Edition)
PML(ProQuest Medical Library)
Science Database (ProQuest)
Biological Science Database
ProQuest Publicly Available Content database
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
ProQuest Central Basic
MEDLINE - Academic
PubMed Central (Full Participant titles)
Directory of Open Access Journals
DatabaseTitle CrossRef
Publicly Available Content Database
ProQuest Central Student
ProQuest Central Essentials
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Central China
ProQuest Central
Health Research Premium Collection
Health and Medicine Complete (Alumni Edition)
Natural Science Collection
ProQuest Central Korea
Biological Science Collection
ProQuest Medical Library (Alumni)
ProQuest Science Journals (Alumni Edition)
ProQuest Biological Science Collection
ProQuest Central Basic
ProQuest Science Journals
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
Health Research Premium Collection (Alumni)
Biological Science Database
ProQuest SciTech Collection
ProQuest Hospital Collection (Alumni)
ProQuest Health & Medical Complete
ProQuest Medical Library
ProQuest One Academic UKI Edition
ProQuest One Academic
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList
CrossRef

Publicly Available Content Database
Database_xml – sequence: 1
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  dbid: BENPR
  name: ProQuest Central
  url: https://www.proquest.com/central
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
EISSN 2050-084X
ExternalDocumentID oai_doaj_org_article_208c79efe15242c0b4dc9b15775668c3
A663848981
10_7554_eLife_65903
GeographicLocations Canada
GeographicLocations_xml – name: Canada
GrantInformation_xml – fundername: ;
  grantid: Endowed Chair AU-0009
– fundername: ;
  grantid: R01GM027750
– fundername: ;
  grantid: R35GM140838
– fundername: ;
  grantid: CBET-1264434
– fundername: ;
  grantid: 18TPA34230046
– fundername: ;
  grantid: 701647
GroupedDBID 3V.
53G
5VS
7X7
88E
88I
8FE
8FH
8FI
8FJ
AAFWJ
AAKDD
AAYXX
ABUWG
ACGFO
ACGOD
ACPRK
ADBBV
ADRAZ
AENEX
AFKRA
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AOIJS
AZQEC
BAWUL
BBNVY
BCNDV
BENPR
BHPHI
BPHCQ
BVXVI
CCPQU
CITATION
DIK
DWQXO
EMOBN
FRP
FYUFA
GNUQQ
GROUPED_DOAJ
GX1
HCIFZ
HMCUK
HYE
IAO
IEA
IHR
INH
INR
ISR
ITC
KQ8
LK8
M1P
M2P
M48
M7P
M~E
NQS
OK1
PGMZT
PIMPY
PQQKQ
PROAC
PSQYO
RHF
RHI
RNS
RPM
UKHRP
AFPKN
7XB
8FK
K9.
PQEST
PQUKI
PRINS
Q9U
7X8
5PM
ID FETCH-LOGICAL-c661t-d46dccc79965e2a2140b383571de3c153ecb75c4c0ab32d6d333f8fb256c3b633
IEDL.DBID RPM
ISSN 2050-084X
IngestDate Tue Dec 17 15:21:30 EST 2024
Tue Sep 17 21:26:25 EDT 2024
Fri Oct 25 04:45:34 EDT 2024
Mon Dec 16 17:32:25 EST 2024
Tue Nov 19 21:04:42 EST 2024
Tue Nov 12 23:24:40 EST 2024
Thu Aug 01 19:48:47 EDT 2024
Fri Dec 06 06:23:18 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Language English
License This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c661t-d46dccc79965e2a2140b383571de3c153ecb75c4c0ab32d6d333f8fb256c3b633
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
These authors contributed equally to this work.
ORCID 0000-0002-3969-6709
0000-0001-7789-5234
0000-0002-7676-0239
0000-0003-0522-9683
0000-0003-4167-8590
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8172240/
PMID 33998458
PQID 2595202862
PQPubID 2045579
ParticipantIDs doaj_primary_oai_doaj_org_article_208c79efe15242c0b4dc9b15775668c3
pubmedcentral_primary_oai_pubmedcentral_nih_gov_8172240
proquest_miscellaneous_2528433370
proquest_journals_2595202862
gale_infotracmisc_A663848981
gale_infotracacademiconefile_A663848981
gale_incontextgauss_ISR_A663848981
crossref_primary_10_7554_eLife_65903
PublicationCentury 2000
PublicationDate 2021-05-17
PublicationDateYYYYMMDD 2021-05-17
PublicationDate_xml – month: 05
  year: 2021
  text: 2021-05-17
  day: 17
PublicationDecade 2020
PublicationPlace Cambridge
PublicationPlace_xml – name: Cambridge
PublicationTitle eLife
PublicationYear 2021
Publisher eLife Science Publications, Ltd
eLife Sciences Publications Ltd
eLife Sciences Publications, Ltd
Publisher_xml – sequence: 0
  name: eLife Sciences Publications Ltd
– name: eLife Science Publications, Ltd
– name: eLife Sciences Publications, Ltd
References McCoy (bib19) 2007; 40
Auffinger (bib3) 2004; 12
Huang (bib13) 2018; 1
Kabsch (bib15) 2010; 66
Basu (bib4) 2019; 26
Smith (bib24) 1987; 91
Sineshchekov (bib21) 2016; 113
Emsley (bib9) 2004; 60
Kim (bib17) 2018; 561
Smith (bib23) 1987; 109
Sineshchekov (bib20) 2015; 112
Kim (bib16) 2016; 7
Assmann (bib2) 2020; 76
Kabsch (bib14) 2010; 66
Yi (bib26) 2016; 55
Bergo (bib6) 2003; 278
Yi (bib27) 2017; 56
Bergo (bib5) 2002; 76
Zondlo (bib28) 2013; 46
Adams (bib1) 2010; 66
Chovancova (bib8) 2012; 8
Huang (bib12) 2016; 72
Huang (bib11) 2015; 71
Li (bib18) 2019; 8
Wojdyla (bib25) 2018; 25
Bergo (bib7) 2004; 43
Govorunova (bib10) 2015; 349
Sineshchekov (bib22) 2019; 117
References_xml – volume: 117
  start-page: 2034
  year: 2019
  ident: bib22
  article-title: Opposite charge movements within the photoactive site modulate two-step channel closing in GtACR1
  publication-title: Biophysical Journal
  doi: 10.1016/j.bpj.2019.10.009
  contributor:
    fullname: Sineshchekov
– volume: 109
  start-page: 3108
  year: 1987
  ident: bib23
  article-title: Vibrational analysis of the all-trans-retinal chromophore in light-adapted bacteriorhodopsin
  publication-title: Journal of the American Chemical Society
  doi: 10.1021/ja00244a038
  contributor:
    fullname: Smith
– volume: 91
  start-page: 804
  year: 1987
  ident: bib24
  article-title: Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin
  publication-title: The Journal of Physical Chemistry
  doi: 10.1021/j100288a011
  contributor:
    fullname: Smith
– volume: 66
  start-page: 133
  year: 2010
  ident: bib14
  article-title: Integration, scaling, space-group assignment and post-refinement
  publication-title: Acta Crystallographica Section D Biological Crystallography
  doi: 10.1107/S0907444909047374
  contributor:
    fullname: Kabsch
– volume: 26
  start-page: 244
  year: 2019
  ident: bib4
  article-title: Automated data collection and real-time data analysis suite for serial synchrotron crystallography
  publication-title: Journal of Synchrotron Radiation
  doi: 10.1107/S1600577518016570
  contributor:
    fullname: Basu
– volume: 112
  start-page: 14236
  year: 2015
  ident: bib20
  article-title: Gating mechanisms of a natural anion channelrhodopsin
  publication-title: PNAS
  doi: 10.1073/pnas.1513602112
  contributor:
    fullname: Sineshchekov
– volume: 66
  start-page: 125
  year: 2010
  ident: bib15
  article-title: XDS
  publication-title: Acta Crystallographica. Section D, Biological Crystallography
  doi: 10.1107/S0907444909047337
  contributor:
    fullname: Kabsch
– volume: 71
  start-page: 1238
  year: 2015
  ident: bib11
  article-title: In meso in situ serial X-ray crystallography of soluble and membrane proteins
  publication-title: Acta Crystallographica Section D Biological Crystallography
  doi: 10.1107/S1399004715005210
  contributor:
    fullname: Huang
– volume: 76
  start-page: 636
  year: 2020
  ident: bib2
  article-title: Making a difference in multi-data-set crystallography: simple and deterministic data-scaling/selection methods
  publication-title: Acta Crystallographica Section D Structural Biology
  doi: 10.1107/S2059798320006348
  contributor:
    fullname: Assmann
– volume: 46
  start-page: 1039
  year: 2013
  ident: bib28
  article-title: Aromatic–Proline Interactions: Electronically Tunable CH/π Interactions
  publication-title: Accounts of Chemical Research
  doi: 10.1021/ar300087y
  contributor:
    fullname: Zondlo
– volume: 66
  start-page: 213
  year: 2010
  ident: bib1
  article-title: PHENIX: a comprehensive Python-based system for macromolecular structure solution
  publication-title: Acta Crystallographica Section D Biological Crystallography
  doi: 10.1107/S0907444909052925
  contributor:
    fullname: Adams
– volume: 40
  start-page: 658
  year: 2007
  ident: bib19
  article-title: Phaser crystallographic software
  publication-title: Journal of Applied Crystallography
  doi: 10.1107/S0021889807021206
  contributor:
    fullname: McCoy
– volume: 76
  start-page: 341
  year: 2002
  ident: bib5
  article-title: A Fourier transform infrared study of Neurospora rhodopsin: similarities with archaeal rhodopsins
  publication-title: Photochemistry and Photobiology
  doi: 10.1562/0031-8655(2002)076<0341:AFTISO>2.0.CO;2
  contributor:
    fullname: Bergo
– volume: 12
  start-page: 379
  year: 2004
  ident: bib3
  article-title: Anion binding to nucleic acids
  publication-title: Structure
  doi: 10.1016/j.str.2004.02.015
  contributor:
    fullname: Auffinger
– volume: 561
  start-page: 343
  year: 2018
  ident: bib17
  article-title: Crystal structure of the natural anion-conducting channelrhodopsin GtACR1
  publication-title: Nature
  doi: 10.1038/s41586-018-0511-6
  contributor:
    fullname: Kim
– volume: 113
  start-page: E1993
  year: 2016
  ident: bib21
  article-title: Photochemical reaction cycle transitions during anion channelrhodopsin gating
  publication-title: PNAS
  doi: 10.1073/pnas.1525269113
  contributor:
    fullname: Sineshchekov
– volume: 25
  start-page: 293
  year: 2018
  ident: bib25
  article-title: DA+ data acquisition and analysis software at the swiss light source macromolecular crystallography beamlines
  publication-title: Journal of Synchrotron Radiation
  doi: 10.1107/S1600577517014503
  contributor:
    fullname: Wojdyla
– volume: 278
  start-page: 36556
  year: 2003
  ident: bib6
  article-title: Conformational changes detected in a sensory rhodopsin II-transducer complex
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.M303719200
  contributor:
    fullname: Bergo
– volume: 72
  start-page: 93
  year: 2016
  ident: bib12
  article-title: In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures
  publication-title: Acta Crystallographica Section D Structural Biology
  doi: 10.1107/S2059798315021683
  contributor:
    fullname: Huang
– volume: 1
  year: 2018
  ident: bib13
  article-title: In situ serial crystallography for rapid de novo membrane protein structure determination
  publication-title: Communications Biology
  doi: 10.1038/s42003-018-0123-6
  contributor:
    fullname: Huang
– volume: 8
  year: 2012
  ident: bib8
  article-title: CAVER 3.0: a tool for the analysis of transport pathways in dynamic protein structures
  publication-title: PLOS Computational Biology
  doi: 10.1371/journal.pcbi.1002708
  contributor:
    fullname: Chovancova
– volume: 60
  start-page: 2126
  year: 2004
  ident: bib9
  article-title: Coot: model-building tools for molecular graphics
  publication-title: Acta Crystallographica. Section D, Biological Crystallography
  doi: 10.1107/S0907444904019158
  contributor:
    fullname: Emsley
– volume: 56
  start-page: 2197
  year: 2017
  ident: bib27
  article-title: Structural changes in an anion channelrhodopsin: formation of the K and L intermediates at 80 K
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.7b00002
  contributor:
    fullname: Yi
– volume: 55
  start-page: 2371
  year: 2016
  ident: bib26
  article-title: Resonance Raman study of an anion channelrhodopsin: effects of mutations near the retinylidene schiff base
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.6b00104
  contributor:
    fullname: Yi
– volume: 349
  start-page: 647
  year: 2015
  ident: bib10
  article-title: NEUROSCIENCE. natural light-gated anion channels: a family of microbial rhodopsins for advanced optogenetics
  publication-title: Science
  doi: 10.1126/science.aaa7484
  contributor:
    fullname: Govorunova
– volume: 8
  year: 2019
  ident: bib18
  article-title: Crystal structure of a natural light-gated anion channelrhodopsin
  publication-title: eLife
  doi: 10.7554/eLife.41741
  contributor:
    fullname: Li
– volume: 7
  year: 2016
  ident: bib16
  article-title: Crystal structure and functional characterization of a light-driven chloride pump having an NTQ motif
  publication-title: Nature Communications
  doi: 10.1038/ncomms12677
  contributor:
    fullname: Kim
– volume: 43
  start-page: 9075
  year: 2004
  ident: bib7
  article-title: Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction
  publication-title: Biochemistry
  doi: 10.1021/bi0361968
  contributor:
    fullname: Bergo
SSID ssj0000748819
Score 2.3816795
Snippet The crystal structure of the light-gated anion channel Gt ACR1 reported in our previous Research Article (Li et al., 2019) revealed a continuous tunnel...
The crystal structure of the light-gated anion channel GtACR1 reported in our previous Research Article (Li et al., 2019) revealed a continuous tunnel...
SourceID doaj
pubmedcentral
proquest
gale
crossref
SourceType Open Website
Open Access Repository
Aggregation Database
SubjectTerms ACR
Binding sites
bromide binding
Channel opening
Channel pores
channelrhodopsin
Chloride
Crystal structure
Crystals
Data collection
Free energy
GtACR1
Guillardia theta
optogenetics
Proteins
Research Advance
Structural Biology and Molecular Biophysics
Structure
SummonAdditionalLinks – databaseName: Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Nb9QwELVQT1wQCBCBgkxViVMgsZPYOW6rloKAQ6FSb5a_AiuxSbWbReLf8ybJVht64MI1nkjJm7HnjTR-w9hxoYN1Ia9R5MQyLUQgydsg0yYIVaustHJQvPn8pbq4Kj5el9d7o76oJ2yUBx6BQ3GuvapjE5FoCuEzVwRfu7xUCkRE-1HnMxN7xdRwBisEZl6PF_IUUua7-GnZxLdVWe_GY00paFDqv3se_90juZd0zh-yBxNb5IvxKx-xe7F9zFZwLffr3-B1P_mo_7pdR9413K271TLE1NGsJP6-X5xe5pw0mhBj3HLq-KB7DL_ALwMfrhLxZctBAXlPKWsVV6id28htC2_xfks9ME_Y1fnZt9OLdJqakHrk2j4NRRW8B2Z1VUZhBSoohzK0VHmI0uOAi96p0hc-s07CN0FK2ejGgft46Sopn7KDtmvjM8arxoLOZMJmuqGBvk7U8DmNAgeJQeWYsOMdkOZmFMcwKCoIbzPgbQa8E3ZCIN-akKL18AB-NpOfzb_8nLAjcpEhzYqWmmK-2-1mYz58vTQLsCZd6Frjg95MRk0H4Lyd7hjgd0jmamZ5OLPEpvLz5V0kmGlTbwwqxVKAj1UiYa9vl-lNalRrY7clG-R7IKqyhKlZBM1-f77SLn8Mwt4abBIM6_n_wOsFuy-o_YaEZtUhO0A0xpfgT717NWyVP232GT8
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: ProQuest Central
  dbid: BENPR
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3fb9MwELage-EFgQBR2JBBk3gKS-Mkdp5QN20MBBMqTNqb5V8ZlWiytSkS_z3fpW4hIPEaX5vk7uz7zjl_x9hhrryxflIhyQlFkmeeKG-9SGqfyUqmhRE9482ni_L8Mv9wVVzFDbdVLKvcron9Qu1bR3vkR4DpBRJ1APC3N7cJdY2ir6uxhcZdtpdNhFIjtnd8evF5tttlQYBUiHmbg3kSofMofJzX4U1ZVNs2WTEU9Yz9_67Lf9dK_hF8zh6w-xE18unGzA_ZndA8YguYmLvlT-C773zDA7teBt7W3C7bxdyHxFLPJP6um57MJpy4muBr3HCq_KDzDD-AMz3vjxTxecMBBXlHoWsRFsihm8BNA6vxbk21MI_Z5dnp15PzJHZPSBxibpf4vPTOOYmEpgiZyZBJWaSjhZz4IBwWuuCsLFzuUmMFbOSFELWqLTCQE7YU4gkbNW0TnjJe1gawJs1Mqmpq7GuzCranluAAM8ggx-xwq0h9syHJ0EguSN-617fu9T1mx6TknQgxW_cX2uW1jhNFZ6nCM4c6AFjkmUtt7l1lJ4WUAJ7K4U9ekYk0cVc0VBxzbdarlX7_ZaanQE8qV5XCA72OQnULxTkTzxrgdYjuaiC5P5DE5HLD4a0n6Di5V_q3K47Zy90w_ZIK1prQrkkGcR8alemYyYEHDV5_ONLMv_UE3wqoEkjr2f9v_pzdy6jAhqhk5T4bwc_CARBSZ1_EafALQSkSxQ
  priority: 102
  providerName: ProQuest
– databaseName: Scholars Portal Journals: Open Access
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Nb9QwELWqIqFeUBEgFlpkUCVOWRI7iZ0TWipKQZRDYaXerPgjZaVuAtksov-eN9ls1RROXONxZM-MPW-k8RvGjlLtS-uTAklOyKJUeKK89TKqvFCFirNS9ow3Z1_y03n66SK72GHbZpyDAlf_TO2on9S8vZr-_nn9Fgce-HWqEA3fhM-LKkzzrCDWz3sCIZFqu84GnN9fyQp-mhSb93l35-yx-xJhWqfU9v1WcOo5_P--qe9WT94KRyf77MGAI_lsY_iHbCfUj9gSRueuvQbiu-IbZth1G3hTcds2y4UPkaUuSvxDNzs-TzixN0ELvORUC0IvHH4BeXrePzLii5oDHPKOgtkyLJFV14GXNezIuzVVxzxm85P3345Po6GfQuQQhbvIp7l3zimkOFkQpUBuZZGgZirxQTpcfcFZlbnUxaWVsJqXUla6skBFTtpcyidst27q8JTxvCoBdGJRxrqiVr9WFPAGahIOeIOccsKOtoo0Pza0GQbpBqne9Ko3veon7B0p-UaEuK77D017aYajY0SsseZQBUCNVLjYpt4VNsmUAhTVDj95RSYyxGZRU7nMZblerczHr-dmBjylU11oLOj1IFQ1UJwrh9cH2A4RYI0kD0aSOG5uPLz1BLP1VoMcMhNAarmYsJc3wzSTStjq0KxJBkgAGlXxhKmRB422Px6pF997ym8NnAns9ey_Zz5ne4KqcYh3Vh2wXbhgOASc6uyL_qj8AQGUITk
  priority: 102
  providerName: Scholars Portal
Title The crystal structure of bromide-bound GtACR1 reveals a pre-activated state in the transmembrane anion tunnel
URI https://www.proquest.com/docview/2595202862
https://search.proquest.com/docview/2528433370
https://pubmed.ncbi.nlm.nih.gov/PMC8172240
https://doaj.org/article/208c79efe15242c0b4dc9b15775668c3
Volume 10
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9NAEF615cIFgQARKNGCKnFy4qwfuz6mUUtBpKoClXKzvA8XS7Vd5YHEv-ebjVPFcOOSQ3YcrWdmd76JZr5h7CxWttB2kiHJcUkQC0uUtzYKSitkJsOkiDzjzfw6vbqNvy6T5RFL9r0wvmjf6GrU3NejpvrpaysfajPe14mNb-YzhaiLSDQ-ZscIvwcpur9-JXxyku168SSi5dh9q0o3SpMspKk5EUKyimnE-0Eg8nz9_97Kf1dKHoSey-fsWYcZ-XS3txfsyDUvWQ0Dc7P6DXR3z3cssNuV423J9aqtK-sCTROT-OfNdLaYcGJqgqfxglPdB3Uz_ALKtNw3FPGq4QCCfEOBq3Y1MujG8aKBzfhmS5Uwr9jt5cWP2VXQzU4IDCLuJrBxao0xEulM4kQhkEdpJKOJnFgXGVxzzmiZmNiEhY5gIRtFUalKDQRkIp1G0Wt20rSNe8N4WhYANaEoQlXSWF8tMlieBoIDyiB_HLCzvSLzhx1FRo7UglSfe9XnXvUDdk5KfhQhXmv_Rbu6yzvr5iJU2LMrHWBFLEyoY2syPUmkBOxUBj_ykUyUE3NFQ6Uxd8V2vc6_fF_kU2AnFatMYUOfOqGyheJM0XUa4HWI7KonedqTxNEy_eW9J-Td0V7nyBcTAVSWigH78LhMT1K5WuPaLckg6kOjMhww2fOg3uv3V-Dtnt678-63__3kO_ZUUOUNcczKU3YCF3TvAZ02eogDs5RD9uT84vpmMfR_QOBzHquhP0R_AC8MHqg
link.rule.ids 230,314,727,780,784,864,885,2102,12056,21388,24318,27924,27925,31719,31720,33744,33745,43310,43805,53791,53793,73745,74302
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Nb9NAEF1BeoALAgEipcCCKnEydby21z6htGpJIY1QaKXeVvvlEonYJR9I_HveOJuAQeLqncT2zOzOm_XsG8YO08Jp4wYlkhyfRWniiPLWiahyiSxlnGnRMt5cTPLRVfrxOrsOG27LUFa5XRPbhdo1lvbIjwDTMyTqAODvb79H1DWKvq6GFhp32R4xp2c9tnd8Ovk83e2yIEAWiHmbg3kSofPIj2eVf5dn5bZNVghFLWP_v-vy37WSfwSfs4fsQUCNfLgx8yN2x9eP2Rwm5nbxE_juG9_wwK4XnjcVN4tmPnM-MtQziX9YDU-mA05cTfA1rjlVftB5hh_AmY63R4r4rOaAgnxFoWvu58iha891Davx1ZpqYZ6wq7PTy5NRFLonRBYxdxW5NHfWWomEJvOJTpBJGaSjmRw4LywWOm-NzGxqY20EbOSEEFVRGWAgK0wuxFPWq5vaP2M8rzRgTZzouKiosa9JStieWoIDzCCD7LPDrSLV7YYkQyG5IH2rVt-q1XefHZOSdyLEbN1eaBY3KkwUlcQFntlXHsAiTWxsUmdLM8ikBPAsLP7kDZlIEXdFTcUxN3q9XKrzL1M1BHoq0qIs8EBvg1DVQHFWh7MGeB2iu-pIHnQkMblsd3jrCSpM7qX67Yp99no3TL-kgrXaN2uSQdyHRmXcZ7LjQZ3X747Us68twXcBVAmktf__m79i90aXF2M1Pp98es7uJ1RsQ7Sy8oD14HP-BdDSyrwMU-IXO34VrQ
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Nb9NAEF1BKiEuCASIlAILqsTJxFnbWfuE0tLQQomqQKXeVt6vEonYJXGQ-Pe8cTYBg8Q1O0ns-dh5Y8--YewwzW2p7bBAkeOyKBWWKG9tEnkrZCHjrExaxptP09HpZfrhKrsK_U-r0Fa53RPbjdrWhp6RDwDTMxTqAOADH9oiLt5N3t58j2iCFL1pDeM0brM9ZMVY9Nje0cn0YrZ74oJkmSP_bQ7pSaTRgTufe_dmlBXbkVkhLbXs_f_u0X_3Tf6RiCb32b2AIPl4Y_IH7JarHrIFzM3N8iew3je-4YRdLx2vPdfLejG3LtI0P4m_b8bHsyEn3ib4HS85dYHQ2YYfwJyWt8eL-LzigIW8oTS2cAvU05XjZQUL8mZNfTGP2OXk5MvxaRQmKUQG-beJbDqyxhiJ4iZzohSoqjRK00wOrUsMNj1ntMxMauJSJ7CXTZLE514DD5lEj5LkMetVdeWeMD7yJSBOLMo49zTkV4sCfkDjwQFsUE322eFWkepmQ5ihUGiQvlWrb9Xqu8-OSMk7EWK5bj-ol9cqBI0ScY5rdt4BZKTCxDq1ptDDTEqA0NzgR16RiRTxWFTkEdflerVSZ59nagwklad5keOCXgchX0NxpgznDnA7RH3VkTzoSCLQTHd56wkqBPpK_XbLPnu5W6ZvUvNa5eo1yQADQKMy7jPZ8aDO7XdXqvnXluw7B8IE6tr__5-_YHcQDer8bPrxKbsrqO-GGGblAevB5dwzAKdGPw8R8QsRQxna
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=The+crystal+structure+of+bromide-bound+GtACR1+reveals+a+pre-activated+state+in+the+transmembrane+anion+tunnel&rft.jtitle=eLife&rft.au=Li%2C+Hai&rft.au=Huang%2C+Chia-Ying&rft.au=Govorunova%2C+Elena+G&rft.au=Sineshchekov%2C+Oleg+A&rft.date=2021-05-17&rft.pub=eLife+Sciences+Publications%2C+Ltd&rft.eissn=2050-084X&rft.volume=10&rft_id=info:doi/10.7554%2FeLife.65903&rft_id=info%3Apmid%2F33998458&rft.externalDBID=PMC8172240
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2050-084X&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2050-084X&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2050-084X&client=summon