4d80: Difference between revisions
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==Metallosphera sedula Vps4 crystal structure== | |||
<StructureSection load='4d80' size='340' side='right'caption='[[4d80]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4d80]] is a 6 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=4D80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D80 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6Å</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=4d80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d80 OCA], [https://pdbe.org/4d80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d80 RCSB], [https://www.ebi.ac.uk/pdbsum/4d80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d80 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A4YHC5_METS5 A4YHC5_METS5] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:26632262</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4d80" style="background-color:#fffaf0;"></div> | ||
[[Category: Boeri-Erba | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Metallosphaera sedula]] | ||
[[Category: | [[Category: Boeri-Erba E]] | ||
[[Category: | [[Category: Caillat C]] | ||
[[Category: Effantin G]] | |||
[[Category: Gottlinger HG]] | |||
[[Category: Macheboeuf P]] | |||
[[Category: McCarthy AA]] | |||
[[Category: Renesto P]] | |||
[[Category: Weissenhorn W]] | |||
[[Category: Wu Y]] | |||
Latest revision as of 14:18, 9 May 2024
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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