Crystallization and low-resolution structure of an effector-caspase/P35 complex: similarities and differences to an initiator-caspase/P35 complex
The aspartate‐specific caspases play a pivotal role in the execution of programmed cell death and therefore constitute important targets for the control of apoptosis. Upon ectopic expression, baculovirus P35 inhibits apoptosis in phylogenetically diverse organisms by suppressing the proteolytic acti...
Saved in:
Published in | Acta crystallographica. Section D, Biological crystallography. Vol. 58; no. 2; pp. 299 - 302 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
Munksgaard International Publishers
01.02.2002
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | The aspartate‐specific caspases play a pivotal role in the execution of programmed cell death and therefore constitute important targets for the control of apoptosis. Upon ectopic expression, baculovirus P35 inhibits apoptosis in phylogenetically diverse organisms by suppressing the proteolytic activity of the cellular caspases in a cleavage‐dependent mechanism. After cleavage by caspase, the P35 fragments remain bound to the target caspase, forming an inhibitory complex that sequesters the caspase from further activity. Crystals of a complex between P35 and Sf‐caspase‐1, an insect effector‐caspase, were grown. A 5.2 Å resolution structure of this inhibitory complex was determined by molecular‐replacement methods. The structure reveals few regions of interaction between the two proteins, much like that observed in the structure of the recently solved human initiator‐caspase/P35 complex. In the effector‐caspase/P35 complex structure presented here, the P35 molecule shifts towards a loop that is conserved in effector caspases but absent in initiator caspase. This shift could strengthen interactions between the two proteins and may explain the preference of P35 for inhibiting effector‐caspases. |
---|---|
AbstractList | The aspartate-specific caspases play a pivotal role in the execution of programmed cell death and therefore constitute important targets for the control of apoptosis. Upon ectopic expression, baculovirus P35 inhibits apoptosis in phylogenetically diverse organisms by suppressing the proteolytic activity of the cellular caspases in a cleavage-dependent mechanism. After cleavage by caspase, the P35 fragments remain bound to the target caspase, forming an inhibitory complex that sequesters the caspase from further activity. Crystals of a complex between P35 and Sf-caspase-1, an insect effector-caspase, were grown. A 5.2 A resolution structure of this inhibitory complex was determined by molecular-replacement methods. The structure reveals few regions of interaction between the two proteins, much like that observed in the structure of the recently solved human initiator-caspase/P35 complex. In the effector-caspase/P35 complex structure presented here, the P35 molecule shifts towards a loop that is conserved in effector caspases but absent in initiator caspase. This shift could strengthen interactions between the two proteins and may explain the preference of P35 for inhibiting effector-caspases. The aspartate‐specific caspases play a pivotal role in the execution of programmed cell death and therefore constitute important targets for the control of apoptosis. Upon ectopic expression, baculovirus P35 inhibits apoptosis in phylogenetically diverse organisms by suppressing the proteolytic activity of the cellular caspases in a cleavage‐dependent mechanism. After cleavage by caspase, the P35 fragments remain bound to the target caspase, forming an inhibitory complex that sequesters the caspase from further activity. Crystals of a complex between P35 and Sf‐caspase‐1, an insect effector‐caspase, were grown. A 5.2 Å resolution structure of this inhibitory complex was determined by molecular‐replacement methods. The structure reveals few regions of interaction between the two proteins, much like that observed in the structure of the recently solved human initiator‐caspase/P35 complex. In the effector‐caspase/P35 complex structure presented here, the P35 molecule shifts towards a loop that is conserved in effector caspases but absent in initiator caspase. This shift could strengthen interactions between the two proteins and may explain the preference of P35 for inhibiting effector‐caspases. |
Author | Friesen, Paul D. Lemongello, Donna Eddins, Michael J. Fisher, Andrew J. |
Author_xml | – sequence: 1 givenname: Michael J. surname: Eddins fullname: Eddins, Michael J. – sequence: 2 givenname: Donna surname: Lemongello fullname: Lemongello, Donna – sequence: 3 givenname: Paul D. surname: Friesen fullname: Friesen, Paul D. – sequence: 4 givenname: Andrew J. surname: Fisher fullname: Fisher, Andrew J. |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11807256$$D View this record in MEDLINE/PubMed |
BookMark | eNqFkctu1TAQhi1URC_wAGxQVuxCbY8TJ-yqQ2-igiLaIlaW64wlgxMfbEft4S36xnV7jgAJIVYee_7vkzyzS7amMCEhLxl9wxiV-59pT6UQoqeMsk428ITsMOj7mlIht_6ot8luSt8opZyDfEa2Geuo5E27Q-4WcZWy9t791NmFqdLTUPlwU0dMwc-PTynH2eQ5YhVs6VdoLZocYm10WuqE--fQVCaMS4-3b6vkRud1dNlherQNruQjTqbcc3gQuKl09T8Mz8lTq33CF5tzj1weHV4sTuqzj8eni4Oz2gjZ8loPXGqBAlrshLC8ZZ2x5VvCgpSD1r3tpaVcALQM-AAA19QYYGA7HARD2COv195lDD9mTFmNLhn0Xk8Y5qQkE0yAECXI1kETQ0oRrVpGN-q4Uoyqhz2ov_ZQmFcb-Xw94vCb2Ay-BLp14MZ5XP3fqA6-vju_pBR4Qes16lLG21-ojt9VK0E26suHY3V1cdW_bz41qoF7Z4Gl9w |
CitedBy_id | crossref_primary_10_1074_jbc_M211607200 crossref_primary_10_1371_journal_pone_0039248 crossref_primary_10_1016_j_virusres_2012_01_012 crossref_primary_10_3390_ijms241713228 crossref_primary_10_1007_s12250_009_3059_7 crossref_primary_10_1007_s13355_016_0403_x crossref_primary_10_1038_sj_onc_1207107 crossref_primary_10_1128_JVI_02065_13 crossref_primary_10_1007_s11262_018_1580_1 crossref_primary_10_1016_S1065_6995_03_00071_4 crossref_primary_10_2217_17460794_3_4_383 crossref_primary_10_1016_j_virol_2015_01_027 |
ContentType | Journal Article |
DBID | BSCLL CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
DOI | 10.1107/S0907444901018753 |
DatabaseName | Istex Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | MEDLINE - Academic MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering Anatomy & Physiology Chemistry |
EISSN | 1399-0047 |
EndPage | 302 |
ExternalDocumentID | 10_1107_S0907444901018753 11807256 AYDPU0032 ark_67375_WNG_VTV9K5Q5_5 |
Genre | miscellaneous Journal Article Comparative Study |
GroupedDBID | --- -ET -~X .3N .GA .Y3 05W 10A 186 1OB 1OC 1Y6 23M 2WC 31~ 33P 36B 3SF 4.4 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5GY 5HH 5LA 66C 6J9 6TJ 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 8WZ 930 A03 A6W AAESR AAEVG AAHHS AANLZ AAONW AASGY AAXRX AAZKR ABCQN ABCUV ABDBF ABEML ABHUG ABJNI ABPTK ABPVW ACAHQ ACBWZ ACCFJ ACCZN ACGFO ACGFS ACNCT ACPOU ACXBN ACXME ACXQS ADAWD ADBBV ADDAD ADEOM ADIYS ADIZJ ADMGS ADOZA ADZOD AEEZP AEIGN AEIMD AEQDE AEUQT AEUYR AFBPY AFEBI AFFPM AFGKR AFPWT AFVGU AFZJQ AGJLS AHBTC AI. AIURR AIWBW AJBDE AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ASPBG ATUGU AUFTA AVWKF AZBYB AZFZN AZVAB BAFTC BDRZF BHBCM BMNLL BNHUX BROTX BRXPI BSCLL BTSUX BY8 CAG COF CS3 D-E D-F DCZOG DPXWK DR2 DRFUL DRSTM EAD EAP EBC EBD EBS EJD EMB EMK EMOBN EST ESX F00 F01 F04 F5P FEDTE G-S G.N GODZA GX1 H.T H.X HF~ HH5 HVGLF HZI HZ~ I-F IHE IX1 J0M K48 LATKE LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MK4 MRFUL MRSTM MSFUL MSSTM MVM MXFUL MXSTM N04 N05 N9A NEJ NF~ O66 P2P P2W P2X P4D PALCI Q.N Q11 QB0 R.K RCJ RIWAO RJQFR RNS ROL RX1 SJN SUPJJ SV3 TN5 TUS UB1 UPT V2E V8K VH1 W8V W99 WBFHL WBKPD WIH WIK WOHZO WQJ WRC WYISQ XFK XG1 ZCG ZZTAW ~02 ~IA ~WT 0R~ AITYG HGLYW CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
ID | FETCH-LOGICAL-c4762-ad27a4e436e844f2618cf1804f377daa9f97f024336132d333b0cc313f8ed41e3 |
IEDL.DBID | DR2 |
ISSN | 1399-0047 0907-4449 |
IngestDate | Sat Aug 17 01:42:30 EDT 2024 Fri Aug 23 03:10:19 EDT 2024 Sat Sep 28 08:38:17 EDT 2024 Sat Aug 24 00:50:53 EDT 2024 Wed Jan 17 05:00:06 EST 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 2 |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c4762-ad27a4e436e844f2618cf1804f377daa9f97f024336132d333b0cc313f8ed41e3 |
Notes | istex:5743562B3F57610D12366503311625CAA400BA99 ArticleID:AYDPU0032 ark:/67375/WNG-VTV9K5Q5-5 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 11807256 |
PQID | 71414344 |
PQPubID | 23479 |
PageCount | 4 |
ParticipantIDs | proquest_miscellaneous_71414344 crossref_primary_10_1107_S0907444901018753 pubmed_primary_11807256 wiley_primary_10_1107_S0907444901018753_AYDPU0032 istex_primary_ark_67375_WNG_VTV9K5Q5_5 |
PublicationCentury | 2000 |
PublicationDate | February 2002 |
PublicationDateYYYYMMDD | 2002-02-01 |
PublicationDate_xml | – month: 02 year: 2002 text: February 2002 |
PublicationDecade | 2000 |
PublicationPlace | 5 Abbey Square, Chester, Cheshire CH1 2HU, England |
PublicationPlace_xml | – name: 5 Abbey Square, Chester, Cheshire CH1 2HU, England – name: United States |
PublicationTitle | Acta crystallographica. Section D, Biological crystallography. |
PublicationTitleAlternate | Acta Cryst. D |
PublicationYear | 2002 |
Publisher | Munksgaard International Publishers |
Publisher_xml | – name: Munksgaard International Publishers |
SSID | ssj0002237 |
Score | 1.6056488 |
Snippet | The aspartate‐specific caspases play a pivotal role in the execution of programmed cell death and therefore constitute important targets for the control of... The aspartate-specific caspases play a pivotal role in the execution of programmed cell death and therefore constitute important targets for the control of... |
SourceID | proquest crossref pubmed wiley istex |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 299 |
SubjectTerms | Animals baculovirus P35 Caspase 1 - chemistry Caspase 1 - metabolism Crystallization Crystallography, X-Ray Cysteine Proteinase Inhibitors - chemistry Cysteine Proteinase Inhibitors - metabolism effector-caspase Humans Inhibitor of Apoptosis Proteins Models, Molecular Protein Conformation Viral Proteins - chemistry Viral Proteins - metabolism |
Title | Crystallization and low-resolution structure of an effector-caspase/P35 complex: similarities and differences to an initiator-caspase/P35 complex |
URI | https://api.istex.fr/ark:/67375/WNG-VTV9K5Q5-5/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1107%2FS0907444901018753 https://www.ncbi.nlm.nih.gov/pubmed/11807256 https://search.proquest.com/docview/71414344 |
Volume | 58 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Nb9QwEB1V5QAcoGyhLBTwAfWAlDaJnTjpbbVQKpCqgrqlnCwntqVVtwnaD9Fy4if0xv_jlzDjJC2lICS4O-M4Ho_fxM9vAJ5Ll5rQ6RJXmjOBsDwN8lyGgYwNoueYFMY8y3cv3R2JN0fJ0RIMu7swjT7ExQ83Whk-XtMC10VbhSRsjhkprxOC-AURoW6MwySoR8Do_aWEFG5_vsAKp9v2oZDtySba2Lpm4credIM-8-nvgOdVHOs3op27YLohNPyT483FvNgsv_yi7vifY1yBOy1QZYPGs-7Bkq16sDqoMEk_OWMbzFNH_T_5HtwcdmXjenD7J4XDVfg2nJ4h_pxM2uueTFeGTerP37-eY57fuj1rRGwXU8tqhy1YQzKpp9iq1BjyZnZrnyfM09_t6TabjU_GmJF7MVhvsSvzgkGPzWsyMSZSlP6jjfsw2nl1MNwN2loQQSkwXgfaxFILK3hqMyEc5n1Z6aIsFI5LabTOXS4dqStyxCex4ZwXYVnyiLvMGhFZ_gCWq7qyD4HFacYL3JXzzGiBcFOT4JFNNSnjx0Ui-vCi8wL1qZH8UD5VCqW6NiF92PB-ctFST4-JKycT9WHvtTo8OMzfJu8SlfThWedICmeEjmV0ZevFTMlIIGgV2O9a41-XveIAJWLSPkTeS_7-Omrw8eX-CCN1_OgfnnkMt3yxG09KX4dlnHz7BDHXvHjqF9UP9I4g5w |
link.rule.ids | 315,786,790,1382,27957,27958,46329,46753 |
linkProvider | Wiley-Blackwell |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LT9wwEB5RONAe-lj62L7woeJQKZDETpz0tlpKt4WuaLVL4WQ5sS2tWJJqHyr0xE_gxv_jl3TsJFBKq0rt3TuJNzPjb-zP3wC84iZWvpE5RppRHtM09tKU-x4PFaLn0CqMOZZvP-4N2Yf9aH8BNpu7MJU-xOWGm40Ml69tgNsN6SrK_eqc0RZ2jFmCQWBh9y1YwrCPXGH1-UpEChdA12KF2vv2PuP12SYa2bhh4trqtGT_6OPfQc_rSNYtRVv3QDeTqBgoh-vzWbaef_9F3_F_Z3kf7tZYlXQq53oAC7powUqnwDr96ISsEcceddvyLVjuNp3jWnDnJ5HDFTjvTk4Qgo7H9Y1PIgtFxuW3i9MzLPVrzyeVju18oklpcASpeCblBEflErPeVG_s0og4Brw-fkOmo6MRFuVOD9ZZbDq9YN4js9KaGFlelPyjjYcw3Ho76Pa8uh2ElzNM2Z5UIZdMMxrrhDGDpV-SmyDxmaGcKylTk3JjBRYpQpRQUUozP89pQE2iFQs0fQSLRVnoJ0DCOKEZLsxpoiRDxCmt5pGOpRXHD7OIteF14wbia6X6IVy15HNx44O0Yc05yuVIOTm0dDkeiS_9d2JvsJduR58iEbVhtfEkgV_EnszIQpfzqeABQ9zK8LmPKwe7eipOkCMsbUPg3OTvryM6B5u7Q0zW4dN_-M0qLPcGH3fEzvv-9jO47XrfOI76c1hER9AvEILNspcuwn4AEIQlCQ |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Nb9QwEB2VVoJyKLClsHzVB9QDUtokduKE22qXpVC0WlC3lJPlxLa06jap9kO0nPoTuPH_-CWMnaSlFIQEd2cSJ2_Gb-LxG4Dn3MTKNzJHTzPKY5rGXppy3-OhQvYcWoUxV-U7iHdH7O1hdLgE3eYsTKUPcfHDzXqGi9fWwU-UqZzcr7YZbV7HmK0vCCzrvgErLKahhXbvw6WGFK5_rsMKtcftfcbrrU00snPNxJXFacW-59PfMc-rRNatRP07oJo5VAUoR9uLebadf_lF3vE_J3kX1mqmSjoVtO7Bki5asN4pMEs_PiNbxNWOup_yLbjVbfrGteD2TxKH6_CtOz1DAjqZ1Oc9iSwUmZSfv59_xUS_xj2pVGwXU01KgyNIVWVSTnFULjHmzfTOkEbE1b_r05dkNj4eY0ru1GCdxabPC0Y9Mi-tibGtipJ_tHEfRv1X-91dr24G4eUMA7YnVcgl04zGOmHMYOKX5CZIfGYo50rK1KTcWHlFigQlVJTSzM9zGlCTaMUCTTdguSgL_RBIGCc0w2U5TZRkyDelVTzSsbTS-GEWsTa8aFAgTirND-FyJZ-Lax-kDVsOJxcj5fTIFsvxSHwcvBYH-wfpXvQ-ElEbNhsgCfwidl9GFrpczAQPGLJWhvd9UOHr8q44QY6ktA2BQ8nfH0d0PvWGIwzV4aN_uGYTbg57ffHuzWDvMay6xjeuQP0JLCMO9FPkX_PsmfOvH3vFI7g |
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=Crystallization+and+low-resolution+structure+of+an+effector-caspase%2FP35+complex%3A+similarities+and+differences+to+an+initiator-caspase%2FP35+complex&rft.jtitle=Acta+crystallographica.+Section+D%2C+Biological+crystallography.&rft.au=Eddins%2C+Michael+J&rft.au=Lemongello%2C+Donna&rft.au=Friesen%2C+Paul+D&rft.au=Fisher%2C+Andrew+J&rft.date=2002-02-01&rft.issn=0907-4449&rft.volume=58&rft.spage=299&rft.epage=302&rft_id=info:doi/10.1107%2FS0907444901018753&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1399-0047&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1399-0047&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1399-0047&client=summon |