2g3k: Difference between revisions

Revision as of 09:14, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2g3k.png

Template:STRUCTURE 2g3k

Crystal structure of the C-terminal domain of Vps28Crystal structure of the C-terminal domain of Vps28

Template:ABSTRACT PUBMED 16749904

About this StructureAbout this Structure

2G3K is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment., Pineda-Molina E, Belrhali H, Piefer AJ, Akula I, Bates P, Weissenhorn W, Traffic. 2006 Aug;7(8):1007-16. Epub 2006 Jun 2. PMID:16749904

Page seeded by OCA on Tue Jul 29 09:14:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2g3k.gif|left|200px]]
+{{Seed}}
+[[Image:2g3k.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2g3k|  PDB=2g3k  |  SCENE=  }}
-'''Crystal structure of the C-terminal domain of Vps28'''
+===Crystal structure of the C-terminal domain of Vps28===
-==Overview==
+<!--
-The endosomal sorting complex I required for transport (ESCRT-I) is composed of the three subunits Vps23/Tsg101, Vps28 and Vps37. ESCRT-I is recruited to cellular membranes during multivesicular endosome biogenesis and by enveloped viruses such as HIV-1 to mediate budding from the cell. Here, we describe the crystal structure of a conserved C-terminal domain from Sacharomyces cerevisiae Vps28 (Vps28-CTD) at 3.05 A resolution which folds independently into a four-helical bundle structure. Co-expression experiments of Vps28-CTD, Vps23 and Vps37 suggest that Vps28-CTD does not directly participate in ESCRT-I assembly and may thus act as an adaptor module for downstream interaction partners. We show through mutagenesis studies that Vps28-CTD employs its strictly conserved surface in the interaction with the ESCRT-III factor Vps20. Furthermore, we present evidence that Vps28-CTD is sufficient to rescue an equine infectious anaemia virus (EIAV) Gag late domain deletion. Vps28-CTD mutations abolishing Vps20 interaction in vitro also prevent the rescue of the EIAV Gag late domain mutant consistent with a potential direct Vps28-ESCRT-III Vps20 recruitment. Therefore, the physiological relevant EIAV Gag-Alix interaction can be functionally replaced by a Gag-Vps28-CTD fusion. Because both Alix and Vps28-CTD can directly recruit ESCRT-III proteins, ESCRT-III assembly coupled to Vps4 action may therefore constitute the minimal budding machinery for EIAV release.
+The line below this paragraph, {{ABSTRACT_PUBMED_16749904}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16749904 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16749904}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Weissenhorn, W.]]
 [[Category: 4 helix bundle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:39:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:14:51 2008''