Reference: Hillig RC, et al. (1999) The crystal structure of rna1p: a new fold for a GTPase-activating protein. Mol Cell 3(6):781-91

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Abstract


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.

Reference Type
Comparative Study | Journal Article | Research Support, Non-U.S. Gov't
Authors
Hillig RC, Renault L, Vetter IR, Drell T, Wittinghofer A, Becker J
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