1yrg
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yrg OCA], [http://www.ebi.ac.uk/pdbsum/1yrg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yrg RCSB]</span> | ||
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[[Category: twinning]] | [[Category: twinning]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:19:11 2008'' |
Revision as of 22:19, 30 March 2008
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| , resolution 2.66Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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