Structural highlights
Function
RNA1_SCHPO GTPase activator for the nuclear Ras-related regulatory protein spi1 (Ran), converting it to the putatively inactive GDP-bound state.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hillig RC, Renault L, Vetter IR, Drell T 4th, Wittinghofer A, Becker J. The crystal structure of rna1p: a new fold for a GTPase-activating protein. Mol Cell. 1999 Jun;3(6):781-91. PMID:10394366
