1YRG

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

Summary for 1YRG

• Entry DOI: 10.2210/pdb1yrg/pdb
• Descriptor: GTPASE-ACTIVATING PROTEIN RNA1_SCHPO (2 entities in total)
• Functional Keywords: gtpase-activating protein, gap, rna1p, rangap, lrr, leucine-rich repeat protein, twinning, hemihedral twinning, merohedral twinning, merohedry, transcription
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Total number of polymer chains: 2
• Total formula weight: 86282.92

Authors

Hillig, R.C.,Renault, L.,Vetter, I.R.,Drell, T.,Wittinghofer, A.,Becker, J. (deposition date: 1999-03-29, release date: 2000-03-29, Last modification date: 2023-12-27)

Primary citation

Hillig, R.C.,Renault, L.,Vetter, I.R.,Drell 4th, T.,Wittinghofer, A.,Becker, J.
The crystal structure of rna1p: a new fold for a GTPase-activating protein.
Mol.Cell, 3:781-791, 1999

PubMed 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.

PubMed: 10394366
DOI: 10.1016/s1097-2765(01)80010-1

Experimental method

X-RAY DIFFRACTION (2.66 Å)