5xmi

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Current revision (10:19, 27 March 2024) (edit) (undo)
 
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<SX load='5xmi' size='340' side='right' viewer='molstar' caption='[[5xmi]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
<SX load='5xmi' size='340' side='right' viewer='molstar' caption='[[5xmi]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xmi]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XMI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XMI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xmi]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XMI FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VPS4, CSC1, DID6, END13, GRD13, VPL4, VPT10, YPR173C, P9705.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xmi OCA], [http://pdbe.org/5xmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xmi RCSB], [http://www.ebi.ac.uk/pdbsum/5xmi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xmi ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xmi OCA], [https://pdbe.org/5xmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xmi RCSB], [https://www.ebi.ac.uk/pdbsum/5xmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xmi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VPS4_YEAST VPS4_YEAST]] Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex.<ref>PMID:11329380</ref> <ref>PMID:9155008</ref> <ref>PMID:9606181</ref>
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[https://www.uniprot.org/uniprot/VPS4_YEAST VPS4_YEAST] Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex.<ref>PMID:11329380</ref> <ref>PMID:9155008</ref> <ref>PMID:9606181</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The cellular ESCRT-III (endosomal sorting complex required for transport-III) and Vps4 (vacuolar protein sorting 4) comprise a common machinery that mediates a variety of membrane remodelling events. Vps4 is essential for the machinery function by using the energy from ATP hydrolysis to disassemble the ESCRT-III polymer into individual proteins. Here, we report the structures of the ATP-bound Vps4E233Q hexamer and its complex with the cofactor Vta1 (vps twenty associated 1) at resolutions of 3.9 and 4.2 A, respectively, determined by electron cryo-microscopy. Six Vps4E233Q subunits in both assemblies exhibit a spiral-shaped ring-like arrangement. Locating at the periphery of the hexameric ring, Vta1 dimer bridges two adjacent Vps4 subunits by two different interaction modes to promote the formation of the active Vps4 hexamer during ESCRT-III filament disassembly. The structural findings, together with the structure-guided biochemical and single-molecule analyses, provide important insights into the process of the ESCRT-III polymer disassembly by Vps4.
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Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution.,Sun S, Li L, Yang F, Wang X, Fan F, Yang M, Chen C, Li X, Wang HW, Sui SF Nat Commun. 2017 Jul 17;8:16064. doi: 10.1038/ncomms16064. PMID:28714467<ref>PMID:28714467</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5xmi" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Baker's yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fan, F]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Li, L]]
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[[Category: Fan F]]
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[[Category: Li, X]]
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[[Category: Li L]]
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[[Category: Sui, S]]
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[[Category: Li X]]
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[[Category: Sun, S]]
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[[Category: Sui S]]
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[[Category: Wang, H]]
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[[Category: Sun S]]
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[[Category: Wang, X]]
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[[Category: Wang H]]
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[[Category: Yang, F]]
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[[Category: Wang X]]
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[[Category: Atpase]]
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[[Category: Yang F]]
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[[Category: Eescrtiii]]
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[[Category: Protein transport]]
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[[Category: Vps4]]
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Current revision

Cryo-EM Structure of the ATP-bound VPS4 mutant-E233Q hexamer (masked)

5xmi, resolution 3.90Å

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