5fvl

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Current revision (13:28, 26 July 2023) (edit) (undo)
 
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<StructureSection load='5fvl' size='340' side='right'caption='[[5fvl]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='5fvl' size='340' side='right'caption='[[5fvl]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fvl]] is a 4 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=5FVL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FVL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fvl]] is a 4 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=5FVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FVL FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fvk|5fvk]]</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]] 1.973&#8491;</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=5fvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvl OCA], [http://pdbe.org/5fvl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fvl RCSB], [http://www.ebi.ac.uk/pdbsum/5fvl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvl 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=5fvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvl OCA], [https://pdbe.org/5fvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fvl RCSB], [https://www.ebi.ac.uk/pdbsum/5fvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvl 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> [[http://www.uniprot.org/uniprot/VPS20_YEAST VPS20_YEAST]] Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Required for the oligomerization of SNF7 into a membrane-associated filament. The VPS20-SNF7 subcomplex is responsible for the membrane association of the ESCRT-III complex. Also required for the RIM101 repressor proteolytic activation.<ref>PMID:11251082</ref> <ref>PMID:11559748</ref> <ref>PMID:12194857</ref> <ref>PMID:12953057</ref> <ref>PMID:15371534</ref>
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[https://www.uniprot.org/uniprot/VPS20_YEAST VPS20_YEAST] Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Required for the oligomerization of SNF7 into a membrane-associated filament. The VPS20-SNF7 subcomplex is responsible for the membrane association of the ESCRT-III complex. Also required for the RIM101 repressor proteolytic activation.<ref>PMID:11251082</ref> <ref>PMID:11559748</ref> <ref>PMID:12194857</ref> <ref>PMID:12953057</ref> <ref>PMID:15371534</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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: Kojima, R]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Mizuguchi, M]]
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[[Category: Kojima R]]
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[[Category: Obita, T]]
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[[Category: Mizuguchi M]]
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[[Category: Onoue, K]]
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[[Category: Obita T]]
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[[Category: Atpase]]
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[[Category: Onoue K]]
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[[Category: Mit domain]]
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[[Category: Viral protein]]
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[[Category: Yeast]]
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Current revision

Crystal structure of Vps4-Vps20 complex from S.cerevisiae

PDB ID 5fvl

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