2e7s
From Proteopedia
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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):245-252. PMID:17292842
Page seeded by OCA on Wed Nov 21 09:59:08 2007
