2p22
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(New page: 200px<br /><applet load="2p22" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p22, resolution 2.70Å" /> '''Structure of the Yea...)
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Revision as of 11:16, 21 November 2007
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Structure of the Yeast ESCRT-I Heterotetramer Core
Overview
The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation, of ubiquitinated transmembrane proteins and the budding of the HIV virus., Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The, crystal structure of the heterotetrameric ESCRT-I complex reveals a highly, asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is, nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk., The stalk is important for cargo sorting by ESCRT-I and is proposed to, serve as a spacer regulating the correct disposition of cargo and other, ESCRT components. Hydrodynamic constraints and crystallographic structures, were used to generate a model of intact ESCRT-I in solution. The results, show how ESCRT-I uses a combination of a rigid stalk and flexible tethers, to interact with lipids, cargo, and other ESCRT complexes over a span of, approximately 25 nm.
About this Structure
2P22 is a Protein complex structure of sequences from Saccharomyces cerevisiae with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer., Kostelansky MS, Schluter C, Tam YY, Lee S, Ghirlando R, Beach B, Conibear E, Hurley JH, Cell. 2007 May 4;129(3):485-98. Epub 2007 Apr 19. PMID:17442384
Page seeded by OCA on Wed Nov 21 13:23:23 2007
