1xb4
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(New page: 200px<br /><applet load="1xb4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xb4, resolution 3.1Å" /> '''Crystal structure of ...)
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Revision as of 03:50, 21 November 2007
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Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II
Overview
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.
About this Structure
1XB4 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
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