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5fvl

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Revision as of 07:39, 6 May 2020

Crystal structure of Vps4-Vps20 complex from S.cerevisiae

Structural highlights

5fvl is a 4 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5fvk
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] [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.^[4] ^[5] ^[6] ^[7] ^[8]

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^[9]

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
↑ Kranz A, Kinner A, Kolling R. A family of small coiled-coil-forming proteins functioning at the late endosome in yeast. Mol Biol Cell. 2001 Mar;12(3):711-23. PMID:11251082
↑ Howard TL, Stauffer DR, Degnin CR, Hollenberg SM. CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins. J Cell Sci. 2001 Jul;114(Pt 13):2395-404. PMID:11559748
↑ Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T, Emr SD. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell. 2002 Aug;3(2):271-82. PMID:12194857
↑ Yeo SC, Xu L, Ren J, Boulton VJ, Wagle MD, Liu C, Ren G, Wong P, Zahn R, Sasajala P, Yang H, Piper RC, Munn AL. Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae. J Cell Sci. 2003 Oct 1;116(Pt 19):3957-70. PMID:12953057 doi:http://dx.doi.org/10.1242/jcs.00751
↑ Xu W, Smith FJ Jr, Subaran R, Mitchell AP. Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans. Mol Biol Cell. 2004 Dec;15(12):5528-37. Epub 2004 Sep 15. PMID:15371534 doi:http://dx.doi.org/10.1091/mbc.E04-08-0666
↑ 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/5fvl"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Vps4-Vps20 complex from S.cerevisiae==
-<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 ==
-<table><tr><td colspan='2'>[[5fvl]] is a 4 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FVL FirstGlance]. <br>
+<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>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fvk|5fvk]]</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=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]</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=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>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 5fvl" 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: Atcc 18824]]
+[[Category: Large Structures]]
 [[Category: Kojima, R]]
 [[Category: Mizuguchi, M]]

5fvl

From Proteopedia

Revision as of 07:39, 6 May 2020

Crystal structure of Vps4-Vps20 complex from S.cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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