1yrg
From Proteopedia
(New page: 200px<br /><applet load="1yrg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yrg, resolution 2.66Å" /> '''THE CRYSTAL STRUCTUR...) |
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- | [[Image:1yrg.gif|left|200px]]<br /><applet load="1yrg" size=" | + | [[Image:1yrg.gif|left|200px]]<br /><applet load="1yrg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yrg, resolution 2.66Å" /> | caption="1yrg, resolution 2.66Å" /> | ||
'''THE CRYSTAL STRUCTURE OF RNA1P: A NEW FOLD FOR A GTPASE-ACTIVATING PROTEIN'''<br /> | '''THE CRYSTAL STRUCTURE OF RNA1P: A NEW FOLD FOR A GTPASE-ACTIVATING PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
- | rna1p is the Schizosaccharomyces pombe ortholog of the mammalian | + | 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== | ==About this Structure== | ||
- | 1YRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http:// | + | 1YRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Becker, J.]] | [[Category: Becker, J.]] | ||
[[Category: Drell, T.]] | [[Category: Drell, T.]] | ||
- | [[Category: Hillig, R | + | [[Category: Hillig, R C.]] |
[[Category: Renault, L.]] | [[Category: Renault, L.]] | ||
- | [[Category: Vetter, I | + | [[Category: Vetter, I R.]] |
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
[[Category: gap]] | [[Category: gap]] | ||
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[[Category: twinning]] | [[Category: twinning]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:24 2008'' |
Revision as of 14:08, 21 February 2008
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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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