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2rkl

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Current revision (09:23, 21 February 2024) (edit) (undo)
 
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<StructureSection load='2rkl' size='340' side='right'caption='[[2rkl]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2rkl' size='340' side='right'caption='[[2rkl]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2rkl]] is a 6 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=2RKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RKL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2rkl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RKL 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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rkk|2rkk]]</div></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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VTA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2rkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rkl OCA], [https://pdbe.org/2rkl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rkl RCSB], [https://www.ebi.ac.uk/pdbsum/2rkl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rkl 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=2rkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rkl OCA], [https://pdbe.org/2rkl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rkl RCSB], [https://www.ebi.ac.uk/pdbsum/2rkl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rkl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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>
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[https://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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rkl ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rkl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The MVB pathway plays essential roles in several eukaryotic cellular processes. Proper function of the MVB pathway requires reversible membrane association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1 regulates the Vps4 activity, but its mechanism of action was poorly understood. We report the high-resolution crystal structures of the Did2- and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1 dimerization and both subunits are required for its function as a Vps4 regulator. Emerging from our analysis is a mechanism of regulation by Vta1 in which the C-terminal domain stabilizes the ATP-dependent double ring assembly of Vps4. In addition, the MIT motif-containing N-terminal domain, projected by a long disordered linker, allows contact between the Vps4 disassembly machinery and the accessory ESCRT-III proteins. This provides an additional level of regulation and coordination for ESCRT-III assembly and disassembly.
 
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Structural basis of Vta1 function in the multivesicular body sorting pathway.,Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z Dev Cell. 2008 Jan;14(1):37-49. PMID:18194651<ref>PMID:18194651</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 2rkl" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Xia, H]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Xiao, J]]
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[[Category: Xia H]]
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[[Category: Xu, Z]]
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[[Category: Xiao J]]
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[[Category: Zhou, J]]
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[[Category: Xu Z]]
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[[Category: Cytoplasm]]
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[[Category: Zhou J]]
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[[Category: Dimerization motif]]
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[[Category: Endosome]]
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[[Category: Lipid transport]]
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[[Category: Membrane]]
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[[Category: Protein transport]]
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[[Category: Transport]]
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Current revision

Crystal Structure of S.cerevisiae Vta1 C-terminal domain

PDB ID 2rkl

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