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3htu

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Revision as of 08:17, 12 December 2018

Crystal structure of the human VPS25-VPS20 subcomplex

Structural highlights

3htu is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	DERP9, EAP20, VPS25 (HUMAN), CHMP6, VPS20 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VPS25_HUMAN] Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. The ESCRT-II complex may be involved in facilitating the budding of certain RNA viruses.^[1] [CHMP6_HUMAN] Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The ESCRT-II-ESCRT-III interaction coordinates the sorting of ubiquitinated cargo with the budding and scission of intralumenal vesicles into multivesicular bodies. The interacting regions of these complexes were mapped to the second winged helix domain of human ESCRT-II subunit VPS25 and the first helix of ESCRT-III subunit VPS20. The crystal structure of this complex was determined at 2.0 A resolution. Residues involved in structural interactions explain the specificity of ESCRT-II for Vps20, and are critical for cargo sorting in vivo. ESCRT-II directly activates ESCRT-III-driven vesicle budding and scission in vitro via these structural interactions. VPS20 and ESCRT-II bind membranes with nanomolar affinity, explaining why binding to ESCRT-II is dispensable for the recruitment of Vps20 to membranes. Docking of the ESCRT-II-VPS20(2) supercomplex reveals a convex membrane-binding surface, suggesting a hypothesis for negative membrane curvature induction in the nascent intralumenal vesicle.

Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis.,Im YJ, Wollert T, Boura E, Hurley JH Dev Cell. 2009 Aug;17(2):234-43. PMID:19686684^[2]

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

References

↑ Pincetic A, Medina G, Carter C, Leis J. Avian sarcoma virus and human immunodeficiency virus, type 1 use different subsets of ESCRT proteins to facilitate the budding process. J Biol Chem. 2008 Oct 31;283(44):29822-30. doi: 10.1074/jbc.M804157200. Epub 2008, Aug 22. PMID:18723511 doi:http://dx.doi.org/10.1074/jbc.M804157200
↑ Im YJ, Wollert T, Boura E, Hurley JH. Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis. Dev Cell. 2009 Aug;17(2):234-43. PMID:19686684 doi:10.1016/j.devcel.2009.07.008

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3htu"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the human VPS25-VPS20 subcomplex==
 <StructureSection load='3htu' size='340' side='right' caption='[[3htu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[3htu]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HTU FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DERP9, EAP20, VPS25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CHMP6, VPS20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3htu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3htu OCA], [http://pdbe.org/3htu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3htu RCSB], [http://www.ebi.ac.uk/pdbsum/3htu PDBsum]</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=3htu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3htu OCA], [http://pdbe.org/3htu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3htu RCSB], [http://www.ebi.ac.uk/pdbsum/3htu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3htu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/3htu_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/3htu_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 3htu" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Vacuolar protein sorting-associated protein|Vacuolar protein sorting-associated protein]]
 == References ==
 <references/>
@@ Line 34: / Line 38: @@
 [[Category: Hurley, J H]]
 [[Category: Im, Y J]]
+[[Category: Coiled coil]]
+[[Category: Cytoplasm]]
 [[Category: Endosome]]
 [[Category: Escrt-ii]]
@@ Line 42: / Line 48: @@
 [[Category: Myristate]]
 [[Category: Nucleus]]
+[[Category: Polymorphism]]
 [[Category: Protein transport]]
 [[Category: Transcription]]

3htu

From Proteopedia

Revision as of 08:17, 12 December 2018

Crystal structure of the human VPS25-VPS20 subcomplex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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