View source for 4d82


==Metallosphera sedula Vps4 crystal structure==
<StructureSection load='4d82' size='340' side='right'caption='[[4d82]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4d82]] is a 3 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=4D82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D82 FirstGlance]. <br>
</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=4d82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d82 OCA], [https://pdbe.org/4d82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d82 RCSB], [https://www.ebi.ac.uk/pdbsum/4d82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d82 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4d82" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Metallosphaera sedula]]
[[Category: Boeri-Erba E]]
[[Category: Caillat C]]
[[Category: Effantin G]]
[[Category: Gottlinger HG]]
[[Category: Macheboeuf P]]
[[Category: McCarthy AA]]
[[Category: Renesto P]]
[[Category: Weissenhorn W]]
[[Category: Wu Y]]