1fkm
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(New page: 200px<br /><applet load="1fkm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fkm, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 12:53, 20 November 2007
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CRYSTAL STRUCTURE OF THE YPT/RAB-GAP DOMAIN OF GYP1P
Overview
We present the 1.9 A resolution crystal structure of the catalytic domain, of Gyp1p, a specific GTPase activating protein (GAP) for Ypt proteins, the, yeast homologues of Rab proteins, which are involved in vesicular, transport. Gyp1p is a member of a large family of eukaryotic proteins with, shared sequence motifs. Previously, no structural information was, available for any member of this class of proteins. The GAP domain of, Gyp1p was found to be fully alpha-helical. However, the observed fold does, not superimpose with other alpha-helical GAPs (e.g. Ras- and, Cdc42/Rho-GAP). The conserved and catalytically crucial arginine residue, identified by mutational analysis, is in a comparable position to the, arginine finger in the Ras- and Cdc42-GAPs, suggesting that Gyp1p utilizes, an arginine finger in the GAP reaction, in analogy to Ras- and Cdc42-GAPs., A model for the interaction between Gyp1p and the Ypt protein satisfying, biochemical data is given.
About this Structure
1FKM is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins., Rak A, Fedorov R, Alexandrov K, Albert S, Goody RS, Gallwitz D, Scheidig AJ, EMBO J. 2000 Oct 2;19(19):5105-13. PMID:11013213
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