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1xb4

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Revision as of 23:07, 10 September 2015

Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II

Structural highlights

1xb4 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.
Gene:	YJR102C, J1957 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[VPS25_YEAST] 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.^[1]

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

BACKGROUND: Down-regulation of plasma membrane receptors via the endocytic pathway involves their monoubiquitylation, transport to endosomal membranes and eventual sorting into multi vesicular bodies (MVB) destined for lysosomal degradation. Successive assemblies of Endosomal Sorting Complexes Required for Transport (ESCRT-I, -II and III) largely mediate sorting of plasma membrane receptors at endosomal membranes, the formation of multivesicular bodies and their release into the endosomal lumen. In addition, the human ESCRT-II has been shown to form a complex with RNA polymerase II elongation factor ELL in order to exert transcriptional control activity. RESULTS: Here we report the crystal structure of Vps25 at 3.1 A resolution. Vps25 crystallizes in a dimeric form and each monomer is composed of two winged helix domains arranged in tandem. Structural comparisons detect no conformational changes between unliganded Vps25 and Vps25 within the ESCRT-II complex composed of two Vps25 copies and one copy each of Vps22 and Vps36 12. CONCLUSIONS: Our structural analyses present a framework for studying Vps25 interactions with ESCRT-I and ESCRT-III partners. Winged helix domain containing proteins have been implicated in nucleic acid binding and it remains to be determined whether Vps25 has a similar activity which might play a role in the proposed transcriptional control exerted by Vps25 and/or the whole ESCRT-II complex.

Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II.,Wernimont AK, Weissenhorn W BMC Struct Biol. 2004 Dec 4;4(1):10. PMID:15579210^[2]

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

References

↑ Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev Cell. 2002 Aug;3(2):283-9. PMID:12194858
↑ Wernimont AK, Weissenhorn W. Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II. BMC Struct Biol. 2004 Dec 4;4(1):10. PMID:15579210 doi:10.1186/1472-6807-4-10

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xb4"

Categories: Atcc 18824 | Weissenhorn, W | Wernimont, A K | Unknown function | Winged helix

@@ Line 2: / Line 2: @@
 <StructureSection load='1xb4' size='340' side='right' caption='[[1xb4]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xb4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XB4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XB4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xb4]] 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=1XB4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XB4 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YJR102C, J1957 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YJR102C, J1957 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1xb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xb4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xb4 RCSB], [http://www.ebi.ac.uk/pdbsum/1xb4 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=1xb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xb4 OCA], [http://pdbe.org/1xb4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xb4 RCSB], [http://www.ebi.ac.uk/pdbsum/1xb4 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1xb4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Saccharomyces cerevisiae]]
+[[Category: Atcc 18824]]
 [[Category: Weissenhorn, W]]
 [[Category: Wernimont, A K]]
 [[Category: Unknown function]]
 [[Category: Winged helix]]

1xb4

From Proteopedia

Revision as of 23:07, 10 September 2015

Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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