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| | ==Crystal Structure of Sulfolobus solfataricus Vps4== | | ==Crystal Structure of Sulfolobus solfataricus Vps4== |
| - | <StructureSection load='4lgm' size='340' side='right' caption='[[4lgm]], [[Resolution|resolution]] 2.71Å' scene=''> | + | <StructureSection load='4lgm' size='340' side='right'caption='[[4lgm]], [[Resolution|resolution]] 2.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lgm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LGM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LGM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lgm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LGM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.711Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSO0909 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4lgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lgm OCA], [https://pdbe.org/4lgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lgm RCSB], [https://www.ebi.ac.uk/pdbsum/4lgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lgm ProSAT]</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=4lgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lgm OCA], [http://pdbe.org/4lgm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lgm RCSB], [http://www.ebi.ac.uk/pdbsum/4lgm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lgm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q97ZJ7_SACS2 Q97ZJ7_SACS2] |
| - | The cellular ESCRT (endosomal sorting complexes required for transport) pathway drives membrane constriction toward the cytosol and effects membrane fission during cytokinesis, endosomal sorting, and the release of many enveloped viruses, including the human immunodeficiency virus. A component of this pathway, the AAA ATPase Vps4, provides energy for pathway progression. Although it is established that Vps4 functions as an oligomer, subunit stoichiometry and other fundamental features of the functional enzyme are unclear. Higher-order oligomers have thus far only been characterized for a Walker B mutant of Vps4 in the presence of ATP. Here, we report that although some mutant Vps4 proteins form dodecameric assemblies, active wild-type Saccharomyces cerevisiae and Sulfolobus solfataricus Vps4 enzymes can form hexamers in the presence of ATP and ADP, as assayed by size-exclusion chromatography and equilibrium analytical ultracentrifugation. The Vta1p activator binds hexameric yeast Vps4p without changing the oligomeric state of Vps4p, implying that the active Vta1p-Vps4p complex also contains a single hexameric ring. Additionally, we report crystal structures of two different archaeal Vps4 homologs, whose structures and lattice interactions suggest a conserved mode of oligomerization. Disruption of the proposed hexamerization interface by mutagenesis abolished the ATPase activity of archaeal Vps4 proteins and blocked Vps4p function in S. cerevisiae. These data challenge the prevailing model that active Vps4 is a double-ring dodecamer and argue that, like other type I AAA ATPases, Vps4 functions as a single ring with six subunits.
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| - | The Oligomeric State of the Active Vps4 AAA ATPase.,Monroe N, Han H, Gonciarz MD, Eckert DM, Karren MA, Whitby FG, Sundquist WI, Hill CP J Mol Biol. 2013 Oct 23. pii: S0022-2836(13)00656-6. doi:, 10.1016/j.jmb.2013.09.043. PMID:24161953<ref>PMID:24161953</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 4lgm" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Sulso]] | + | [[Category: Large Structures]] |
| - | [[Category: Vesicle-fusing ATPase]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Han, H]] | + | [[Category: Han H]] |
| - | [[Category: Hill, C P]] | + | [[Category: Hill CP]] |
| - | [[Category: Monroe, N]] | + | [[Category: Monroe N]] |
| - | [[Category: Whitby, F G]] | + | [[Category: Whitby FG]] |
| - | [[Category: Atp hydrolysis]]
| + | |
| - | [[Category: Hydrolase]]
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