4d81: Difference between revisions
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<StructureSection load='4d81' size='340' side='right'caption='[[4d81]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4d81' size='340' side='right'caption='[[4d81]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4d81]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4d81]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Metallosphaera_sedula Metallosphaera sedula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D81 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=4d81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d81 OCA], [https://pdbe.org/4d81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d81 RCSB], [https://www.ebi.ac.uk/pdbsum/4d81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d81 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/A4YHC5_METS5 A4YHC5_METS5]] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Metallosphaera sedula]] | ||
[[Category: Boeri-Erba | [[Category: Boeri-Erba E]] | ||
[[Category: Caillat | [[Category: Caillat C]] | ||
[[Category: Effantin | [[Category: Effantin G]] | ||
[[Category: Gottlinger | [[Category: Gottlinger HG]] | ||
[[Category: Macheboeuf | [[Category: Macheboeuf P]] | ||
[[Category: McCarthy | [[Category: McCarthy AA]] | ||
[[Category: Renesto | [[Category: Renesto P]] | ||
[[Category: Weissenhorn | [[Category: Weissenhorn W]] | ||
[[Category: Wu | [[Category: Wu Y]] | ||
Revision as of 10:51, 14 September 2022
Metallosphera sedula Vps4 crystal structureMetallosphera sedula Vps4 crystal structure
Structural highlights
FunctionPublication Abstract from PubMedThe vacuolar protein sorting 4 AAA-ATPase (Vps4) recycles endosomal sorting complexes required for transport (ESCRT-III) polymers from cellular membranes. Here we present a 3.6-A X-ray structure of ring-shaped Vps4 from Metallosphera sedula (MsVps4), seen as an asymmetric pseudohexamer. Conserved key interface residues are shown to be important for MsVps4 assembly, ATPase activity in vitro, ESCRT-III disassembly in vitro and HIV-1 budding. ADP binding leads to conformational changes within the protomer, which might propagate within the ring structure. All ATP-binding sites are accessible and the pseudohexamer binds six ATP with micromolar affinity in vitro. In contrast, ADP occupies one high-affinity and five low-affinity binding sites in vitro, consistent with conformational asymmetry induced on ATP hydrolysis. The structure represents a snapshot of an assembled Vps4 conformation and provides insight into the molecular motions the ring structure undergoes in a concerted action to couple ATP hydrolysis to ESCRT-III substrate disassembly. Asymmetric ring structure of Vps4 required for ESCRT-III disassembly.,Caillat C, Macheboeuf P, Wu Y, McCarthy AA, Boeri-Erba E, Effantin G, Gottlinger HG, Weissenhorn W, Renesto P Nat Commun. 2015 Dec 3;6:8781. doi: 10.1038/ncomms9781. PMID:26632262[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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