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| | ==Crystal Structure of the Vps4p-dimer== | | ==Crystal Structure of the Vps4p-dimer== |
| - | <StructureSection load='2rko' size='340' side='right' caption='[[2rko]], [[Resolution|resolution]] 3.35Å' scene=''> | + | <StructureSection load='2rko' size='340' side='right'caption='[[2rko]], [[Resolution|resolution]] 3.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rko]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RKO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RKO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rko]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RKO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xwi|1xwi]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xwi|1xwi]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VPS4P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VPS4P ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2rko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rko OCA], [http://pdbe.org/2rko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rko RCSB], [http://www.ebi.ac.uk/pdbsum/2rko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rko ProSAT]</span></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=2rko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rko OCA], [https://pdbe.org/2rko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rko RCSB], [https://www.ebi.ac.uk/pdbsum/2rko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rko ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [[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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2rko" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2rko" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 18824]] | | [[Category: Atcc 18824]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Gruetter, M G]] | | [[Category: Gruetter, M G]] |
| | [[Category: Hartmann, C]] | | [[Category: Hartmann, C]] |
| Structural highlights
Function
[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.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The vacuolar protein sorting (Vps) pathway, in which Vps4 class I AAA-ATPases play a central role, regulates growth factor receptors, immune response, and developmental signaling, and participates in tumor suppression, apoptosis, and retrovirus budding. We present the first atomic structure of the nucleotide-free yeast His(6)DeltaNVps4p dimer and its AMPPNP (5'-adenylyl-beta,gamma-imidodiphosphate)-bound tetradecamer, derived from a cryo electron microscopy map. Vps4p dimers form two distinct heptameric rings and accommodate AAA cassettes in a head-to-head--not in a head-to-tail-fashion as in class II AAA-ATPases. Our model suggests a mechanism for disassembling ESCRT (endosomal sorting complex required for transport) complexes by movements of substrate-binding domains located at the periphery of the tetradecamer during ATP hydrolysis in one ring, followed by translocation through the central pore and ATP hydrolysis in the second ring.
Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p.,Hartmann C, Chami M, Zachariae U, de Groot BL, Engel A, Grutter MG J Mol Biol. 2008 Mar 21;377(2):352-63. Epub 2008 Jan 15. PMID:18272179[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zahn R, Stevenson BJ, Schroder-Kohne S, Zanolari B, Riezman H, Munn AL. End13p/Vps4p is required for efficient transport from early to late endosomes in Saccharomyces cerevisiae. J Cell Sci. 2001 May;114(Pt 10):1935-47. PMID:11329380
- ↑ Babst M, Sato TK, Banta LM, Emr SD. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 1997 Apr 15;16(8):1820-31. PMID:9155008 doi:10.1093/emboj/16.8.1820
- ↑ Babst M, Wendland B, Estepa EJ, Emr SD. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 1998 Jun 1;17(11):2982-93. PMID:9606181 doi:10.1093/emboj/17.11.2982
- ↑ Hartmann C, Chami M, Zachariae U, de Groot BL, Engel A, Grutter MG. Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p. J Mol Biol. 2008 Mar 21;377(2):352-63. Epub 2008 Jan 15. PMID:18272179 doi:10.1016/j.jmb.2008.01.010
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