2pjw
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(New page: 200px<br /><applet load="2pjw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pjw, resolution 3.01Å" /> '''The Vps27/Hse1 compl...)
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Revision as of 11:26, 21 November 2007
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The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting
Overview
The yeast Vps27/Hse1 complex and the homologous mammalian Hrs/STAM complex, deliver ubiquitinated transmembrane proteins to the ESCRT, endosomal-sorting pathway. The Vps27/Hse1 complex directly binds to, ubiquitinated transmembrane proteins and recruits both ubiquitin ligases, and deubiquitinating enzymes. We have solved the crystal structure of the, core responsible for the assembly of the Vps27/Hse1 complex at 3.0 A, resolution. The structure consists of two intertwined GAT domains, each, consisting of two helices from one subunit and one from the other. The two, GAT domains are connected by an antiparallel coiled coil, forming a 90, A-long barbell-like structure. This structure places the domains of Vps27, and Hse1 that recruit ubiquitinated cargo and deubiquitinating enzymes, close to each other. Coarse-grained Monte Carlo simulations of the, Vps27/Hse1 complex on a membrane show how the complex binds cooperatively, to lipids and ubiquitinated membrane proteins and acts as a scaffold for, ubiquitination reactions.
About this Structure
2PJW is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The Vps27/Hse1 Complex Is a GAT Domain-Based Scaffold for Ubiquitin-Dependent Sorting., Prag G, Watson H, Kim YC, Beach BM, Ghirlando R, Hummer G, Bonifacino JS, Hurley JH, Dev Cell. 2007 Jun;12(6):973-86. PMID:17543868
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