2nty
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(New page: 200px<br /><applet load="2nty" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nty, resolution 3.100Å" /> '''Rop4-GDP-PRONE8'''<...)
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Revision as of 10:46, 21 November 2007
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Rop4-GDP-PRONE8
Overview
Rho of plants (Rop) proteins belong to the superfamily of small, GTP-binding (G) proteins and are vital regulators of signal transduction, in plants. In order to become activated, Rop proteins need to exchange GDP, for GTP, an intrinsically slow process catalyzed by guanine nucleotide, exchange factors (GEFs). RopGEFs show no homology to animal RhoGEFs, and, the catalytic mechanism remains elusive. GEF-catalysed nucleotide exchange, proceeds via transient ternary and stable binary complexes. While a number, of structural studies have analyzed binary nucleotide-free G protein-GEF, complexes, very little is known about the ternary complexes. Here we, report the X-ray structure of the catalytic PRONE domain of RopGEF8 from, Arabidopsis thaliana, both alone and in a ternary complex with Rop4 and, GDP. The features of the latter complex, a transient intermediate of the, exchange reaction never directly observed before, suggest a common, mechanism of catalyzed nucleotide exchange applicable to small G proteins, in general.
About this Structure
2NTY is a Protein complex structure of sequences from Arabidopsis thaliana with GDP as ligand. Full crystallographic information is available from OCA.
Reference
Structural evidence for a common intermediate in small G protein-GEF reactions., Thomas C, Fricke I, Scrima A, Berken A, Wittinghofer A, Mol Cell. 2007 Jan 12;25(1):141-9. PMID:17218277
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