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1yrg

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Image:1yrg.gif

1yrg, resolution 2.66Å

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THE CRYSTAL STRUCTURE OF RNA1P: A NEW FOLD FOR A GTPASE-ACTIVATING PROTEIN

Overview

rna1p is the Schizosaccharomyces pombe ortholog of the mammalian, GTPase-activating protein (GAP) of Ran. Both proteins are essential for, nuclear transport. Here, we report the crystal structure of rna1p at 2.66, A resolution. It contains 11 leucine-rich repeats that adopt the, nonglobular shape of a crescent, bearing no resemblance to RhoGAP or, RasGAP. The invariant residues of RanGAP form a contiguous surface, strongly indicating the Ran-binding interface. Alanine mutations identify, Arg-74 as a critical residue for GTP hydrolysis. In contrast to RasGAP and, RhoGAP, Arg-74 could be substituted by lysine and contributed, significantly to the binding of Ran. Therefore, we suggest a GAP mechanism, for rna1p, which constitutes a variation of the arginine finger mechanism, found for Ras GAP and RhoGAP.

About this Structure

1YRG is a Single protein structure of sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.

Reference

The crystal structure of rna1p: a new fold for a GTPase-activating protein., Hillig RC, Renault L, Vetter IR, Drell T 4th, Wittinghofer A, Becker J, Mol Cell. 1999 Jun;3(6):781-91. PMID:10394366

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