2e7s
From Proteopedia
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'''Crystal structure of the yeast Sec2p GEF domain''' | '''Crystal structure of the yeast Sec2p GEF domain''' | ||
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[[Category: Nureki, O.]] | [[Category: Nureki, O.]] | ||
[[Category: Sato, Y.]] | [[Category: Sato, Y.]] | ||
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Revision as of 23:05, 3 May 2008
Crystal structure of the yeast Sec2p GEF domain
Overview
Vesicular traffic during exocytosis is regulated by Rab GTPase, Sec4p in yeast, which is activated by a guanine nucleotide exchange factor (GEF) called Sec2p. The GEF activity is localized in the N-terminal 160 residues of Sec2p, which lacks sequence similarity with any other GEFs with known structures, and thereby the guanine nucleotide exchange mechanism by Sec2p remains unknown. Here, we report the crystal structure of the Sec2p GEF domain at 3.0 A resolution. The structure unexpectedly consists of a homodimeric, parallel coiled coil that extends over 180 A. Pull-down and guanine nucleotide exchange analyses on a series of deletion and point mutants of Sec2p unveiled the catalytic residues for its GEF activity as well as the Sec4p binding site, thus presenting a nucleotide exchange mechanism by a simple coiled coil. The present functional analyses allow us to build the Sec2p:Sec4p complex model, which explains the specificity for Rab GTPases by their respective GEF proteins.
About this Structure
2E7S is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Asymmetric coiled-coil structure with Guanine nucleotide exchange activity., Sato Y, Shirakawa R, Horiuchi H, Dohmae N, Fukai S, Nureki O, Structure. 2007 Feb;15(2):245-52. PMID:17292842 Page seeded by OCA on Sun May 4 02:05:46 2008
