8jo0: Difference between revisions
New page: '''Unreleased structure''' The entry 8jo0 is ON HOLD Authors: Yini, L., Yigong, S. Description: The Cryo-EM structure of a heptameric CED-4/CED-3 catalytic complex [[Category: Unreleas... |
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The | ==The Cryo-EM structure of a heptameric CED-4/CED-3 catalytic complex== | ||
<StructureSection load='8jo0' size='340' side='right'caption='[[8jo0]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8jo0]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JO0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8jo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jo0 OCA], [https://pdbe.org/8jo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jo0 RCSB], [https://www.ebi.ac.uk/pdbsum/8jo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jo0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CED4_CAEEL CED4_CAEEL] Isoform a plays a major role in programmed cell death (PCD, apoptosis). Egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3. Isoform b prevents PCD.<ref>PMID:1286611</ref> <ref>PMID:8706125</ref> <ref>PMID:9027313</ref> <ref>PMID:10688797</ref> <ref>PMID:15383288</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Caenorhabditis elegans (C. elegans), onset of programmed cell death is marked with the activation of CED-3, a process that requires assembly of the CED-4 apoptosome. Activated CED-3 forms a holoenzyme with the CED-4 apoptosome to cleave a wide range of substrates, leading to irreversible cell death. Despite decades of investigations, the underlying mechanism of CED-4-facilitated CED-3 activation remains elusive. Here, we report cryo-EM structures of the CED-4 apoptosome and three distinct CED-4/CED-3 complexes that mimic different activation stages for CED-3. In addition to the previously reported octamer in crystal structures, CED-4, alone or in complex with CED-3, exists in multiple oligomeric states. Supported by biochemical analyses, we show that the conserved CARD-CARD interaction promotes CED-3 activation, and initiation of programmed cell death is regulated by the dynamic organization of the CED-4 apoptosome. | |||
Structural insights into CED-3 activation.,Li Y, Tian L, Zhang Y, Shi Y Life Sci Alliance. 2023 Jul 4;6(9):e202302056. doi: 10.26508/lsa.202302056. Print , 2023 Sep. PMID:37402593<ref>PMID:37402593</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8jo0" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caenorhabditis elegans]] | |||
[[Category: Large Structures]] | |||
[[Category: Li Y]] | |||
[[Category: Shi Y]] | |||
Latest revision as of 10:40, 3 July 2024
The Cryo-EM structure of a heptameric CED-4/CED-3 catalytic complexThe Cryo-EM structure of a heptameric CED-4/CED-3 catalytic complex
Structural highlights
FunctionCED4_CAEEL Isoform a plays a major role in programmed cell death (PCD, apoptosis). Egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3. Isoform b prevents PCD.[1] [2] [3] [4] [5] Publication Abstract from PubMedIn Caenorhabditis elegans (C. elegans), onset of programmed cell death is marked with the activation of CED-3, a process that requires assembly of the CED-4 apoptosome. Activated CED-3 forms a holoenzyme with the CED-4 apoptosome to cleave a wide range of substrates, leading to irreversible cell death. Despite decades of investigations, the underlying mechanism of CED-4-facilitated CED-3 activation remains elusive. Here, we report cryo-EM structures of the CED-4 apoptosome and three distinct CED-4/CED-3 complexes that mimic different activation stages for CED-3. In addition to the previously reported octamer in crystal structures, CED-4, alone or in complex with CED-3, exists in multiple oligomeric states. Supported by biochemical analyses, we show that the conserved CARD-CARD interaction promotes CED-3 activation, and initiation of programmed cell death is regulated by the dynamic organization of the CED-4 apoptosome. Structural insights into CED-3 activation.,Li Y, Tian L, Zhang Y, Shi Y Life Sci Alliance. 2023 Jul 4;6(9):e202302056. doi: 10.26508/lsa.202302056. Print , 2023 Sep. PMID:37402593[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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