1yrg

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(New page: 200px<br /><applet load="1yrg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yrg, resolution 2.66&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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[[Image:1yrg.gif|left|200px]]<br /><applet load="1yrg" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yrg.gif|left|200px]]<br /><applet load="1yrg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1yrg, resolution 2.66&Aring;" />
caption="1yrg, resolution 2.66&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YRG OCA].
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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.]]
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[[Category: Hillig, R.C.]]
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[[Category: Hillig, R C.]]
[[Category: Renault, L.]]
[[Category: Renault, L.]]
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[[Category: Vetter, I.R.]]
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[[Category: Vetter, I R.]]
[[Category: Wittinghofer, A.]]
[[Category: Wittinghofer, A.]]
[[Category: gap]]
[[Category: gap]]
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[[Category: twinning]]
[[Category: twinning]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:00:07 2007''
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''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


1yrg, resolution 2.66Å

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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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