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| <SX load='6oo2' size='340' side='right' viewer='molstar' caption='[[6oo2]], [[Resolution|resolution]] 4.40Å' scene=''> | | <SX load='6oo2' size='340' side='right' viewer='molstar' caption='[[6oo2]], [[Resolution|resolution]] 4.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6oo2]] is a 19 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=6OO2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OO2 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6oo2]] is a 19 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OO2 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>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4Å</td></tr> |
| <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| <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=4932 ATCC 18824]), VTA1, YLR181C ([http://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'>[https://proteopedia.org/fgij/fg.htm?mol=6oo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oo2 OCA], [https://pdbe.org/6oo2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oo2 RCSB], [https://www.ebi.ac.uk/pdbsum/6oo2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oo2 ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6oo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oo2 OCA], [http://pdbe.org/6oo2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oo2 RCSB], [http://www.ebi.ac.uk/pdbsum/6oo2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oo2 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> [[http://www.uniprot.org/uniprot/VTA1_YEAST VTA1_YEAST]] Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting the plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of VSP4, promotes the oligomerization of VPS4 and stimulates its ATPase activity by 6- to 8-fold.<ref>PMID:12953057</ref> <ref>PMID:14701806</ref> <ref>PMID:16505166</ref> <ref>PMID:16601096</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> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Many AAA+ ATPases form hexamers that unfold protein substrates by translocating them through their central pore. Multiple structures have shown how a helical assembly of subunits binds a single strand of substrate, and indicate that translocation results from the ATP-driven movement of subunits from one end of the helical assembly to the other end. To understand how more complex substrates are bound and translocated, we demonstrated that linear and cyclic versions of peptides bind to the S. cerevisiae AAA+ ATPase Vps4 with similar affinities, and determined cryo-EM structures of cyclic peptide complexes. The peptides bind in a hairpin conformation, with one primary strand equivalent to the single chain peptide ligands, while the second strand returns through the translocation pore without making intimate contacts with Vps4. These observations indicate a general mechanism by which AAA+ ATPases may translocate a variety of substrates that include extended chains, hairpins, and crosslinked polypeptide chains.
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| Structure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases.,Han H, Fulcher JM, Dandey VP, Iwasa JH, Sundquist WI, Kay MS, Shen PS, Hill CP Elife. 2019 Jun 11;8. pii: 44071. doi: 10.7554/eLife.44071. PMID:31184588<ref>PMID:31184588</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6oo2" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: Atcc 18824]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Dandey, V P]] | | [[Category: Saccharomyces cerevisiae]] |
| [[Category: Fulcher, J M]] | | [[Category: Synthetic construct]] |
| [[Category: Han, H]] | | [[Category: Dandey VP]] |
| [[Category: Hill, C P]] | | [[Category: Fulcher JM]] |
| [[Category: Kay, M S]] | | [[Category: Han H]] |
| [[Category: Shen, P]] | | [[Category: Hill CP]] |
| [[Category: Sundquist, W I]] | | [[Category: Kay MS]] |
| [[Category: Aaa atpase]] | | [[Category: Shen P]] |
| [[Category: Escrt]] | | [[Category: Sundquist WI]] |
| [[Category: Transport protein]]
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| [[Category: Vps4]]
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| [[Category: Vta1]]
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