4d82: Difference between revisions
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==Metallosphera sedula Vps4 crystal structure== | ==Metallosphera sedula Vps4 crystal structure== | ||
<StructureSection load='4d82' size='340' side='right' caption='[[4d82]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='4d82' size='340' side='right'caption='[[4d82]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4d82]] is a 3 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D82 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4d82]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51363 Atcc 51363]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D82 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> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d81|4d81]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d81|4d81]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Vesicle-fusing_ATPase Vesicle-fusing ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.6 3.6.4.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Vesicle-fusing_ATPase Vesicle-fusing ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.6 3.6.4.6] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d82 OCA], [http://pdbe.org/4d82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d82 RCSB], [http://www.ebi.ac.uk/pdbsum/4d82 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d82 OCA], [http://pdbe.org/4d82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d82 RCSB], [http://www.ebi.ac.uk/pdbsum/4d82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d82 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 51363]] | |||
[[Category: Large Structures]] | |||
[[Category: Vesicle-fusing ATPase]] | [[Category: Vesicle-fusing ATPase]] | ||
[[Category: Boeri-Erba, E]] | [[Category: Boeri-Erba, E]] | ||
Revision as of 10:49, 27 March 2019
Metallosphera sedula Vps4 crystal structureMetallosphera sedula Vps4 crystal structure
Structural highlights
Publication 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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