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5fvk

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Revision as of 07:39, 6 May 2020

Crystal structure of Vps4-Vfa1 complex from S.cerevisiae at 1.66 A resolution.

Structural highlights

5fvk is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5fvl
Activity:	Vesicle-fusing ATPase, with EC number 3.6.4.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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] [VFA1_YEAST] VPS4-associated protein involved in trafficking to the vacuole.

Publication Abstract from PubMed

The endosomal sorting complex required for transport (ESCRT) facilitates roles in membrane remodeling, such as multivesicular body biogenesis, enveloped virus budding and cell division. In yeast, Vps4 plays a crucial role in intraluminal vesicle formation by disassembling ESCRT proteins. Vps4 is recruited by ESCRT-III proteins to the endosomal membrane through the interaction between the microtubule interacting and trafficking (MIT) domain of Vps4 and the C-terminal MIT-interacting motif (MIM) of ESCRT-III proteins. Here, we have determined the crystal structure of Vps4-MIT in a complex with Vps20, a member of ESCRT-III, and revealed that Vps20 adopts a unique MIM2 conformation. Based on structural comparisons with other known MIM2s, we have refined the consensus sequence of MIM2. We have shown that another ESCRT-III protein, Ist1, binds to Vps4-MIT via its C-terminal MIM1 with higher affinity than Vps2, but lacks MIM2 by surface plasmon resonance. Surprisingly, the Ist1 MIM1 competed with the MIM2 of Vfa1, a regulator of Vps4, for binding to Vps4-MIT, even though these MIMs bind in non-overlapping sites on the MIT. These findings provide insight into the allosteric recognition of MIMs of ESCRT-III by Vps4 and also the regulation of ESCRT machinery at the last step of membrane remodeling.

Structural Fine-Tuning of MIT-Interacting Motif 2 (MIM2) and Allosteric Regulation of ESCRT-III by Vps4 in Yeast.,Kojima R, Obita T, Onoue K, Mizuguchi M J Mol Biol. 2016 Apr 10. pii: S0022-2836(16)30051-1. doi:, 10.1016/j.jmb.2016.04.007. PMID:27075672^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Kojima R, Obita T, Onoue K, Mizuguchi M. Structural Fine-Tuning of MIT-Interacting Motif 2 (MIM2) and Allosteric Regulation of ESCRT-III by Vps4 in Yeast. J Mol Biol. 2016 Apr 10. pii: S0022-2836(16)30051-1. doi:, 10.1016/j.jmb.2016.04.007. PMID:27075672 doi:http://dx.doi.org/10.1016/j.jmb.2016.04.007

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5fvk"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Vps4-Vfa1 complex from S.cerevisiae at 1.66 A resolution.==
-<StructureSection load='5fvk' size='340' side='right' caption='[[5fvk]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
+<StructureSection load='5fvk' size='340' side='right'caption='[[5fvk]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5fvk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FVK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5fvk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FVK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FVK FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fvl|5fvl]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvk OCA], [http://pdbe.org/5fvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fvk RCSB], [http://www.ebi.ac.uk/pdbsum/5fvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvk 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=5fvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvk OCA], [http://pdbe.org/5fvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fvk RCSB], [http://www.ebi.ac.uk/pdbsum/5fvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvk ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5fvk" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Vesicle-fusing ATPase]]
 [[Category: Kojima, R]]

5fvk

From Proteopedia

Revision as of 07:39, 6 May 2020

Crystal structure of Vps4-Vfa1 complex from S.cerevisiae at 1.66 A resolution.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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