1k5d
From Proteopedia
(New page: 200px<br /> <applet load="1k5d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k5d, resolution 2.70Å" /> '''Crystal structure o...) |
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| - | [[Image:1k5d.gif|left|200px]]<br /> | + | [[Image:1k5d.gif|left|200px]]<br /><applet load="1k5d" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1k5d" size=" | + | |
caption="1k5d, resolution 2.70Å" /> | caption="1k5d, resolution 2.70Å" /> | ||
'''Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex'''<br /> | '''Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | GTPase-activating proteins (GAPs) increase the rate of GTP hydrolysis on | + | GTPase-activating proteins (GAPs) increase the rate of GTP hydrolysis on guanine nucleotide-binding proteins by many orders of magnitude. Studies with Ras and Rho have elucidated the mechanism of GAP action by showing that their catalytic machinery is both stabilized by GAP binding and complemented by the insertion of a so-called 'arginine finger' into the phosphate-binding pocket. This has been proposed as a universal mechanism for GAP-mediated GTP hydrolysis. Ran is a nuclear Ras-related protein that regulates both transport between the nucleus and cytoplasm during interphase, and formation of the mitotic spindle and/or nuclear envelope in dividing cells. Ran-GTP is hydrolysed by the combined action of Ran-binding proteins (RanBPs) and RanGAP. Here we present the three-dimensional structure of a Ran-RanBP1-RanGAP ternary complex in the ground state and in a transition-state mimic. The structure and biochemical experiments show that RanGAP does not act through an arginine finger, that the basic machinery for fast GTP hydrolysis is provided exclusively by Ran and that correct positioning of the catalytic glutamine is essential for catalysis. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K5D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1K5D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Schizosaccharomyces pombe]] | [[Category: Schizosaccharomyces pombe]] | ||
[[Category: Koerner, C.]] | [[Category: Koerner, C.]] | ||
| - | [[Category: Seewald, M | + | [[Category: Seewald, M J.]] |
| - | [[Category: Vetter, I | + | [[Category: Vetter, I R.]] |
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
[[Category: GNP]] | [[Category: GNP]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:20 2008'' |
Revision as of 11:30, 21 February 2008
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Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex
Contents |
Overview
GTPase-activating proteins (GAPs) increase the rate of GTP hydrolysis on guanine nucleotide-binding proteins by many orders of magnitude. Studies with Ras and Rho have elucidated the mechanism of GAP action by showing that their catalytic machinery is both stabilized by GAP binding and complemented by the insertion of a so-called 'arginine finger' into the phosphate-binding pocket. This has been proposed as a universal mechanism for GAP-mediated GTP hydrolysis. Ran is a nuclear Ras-related protein that regulates both transport between the nucleus and cytoplasm during interphase, and formation of the mitotic spindle and/or nuclear envelope in dividing cells. Ran-GTP is hydrolysed by the combined action of Ran-binding proteins (RanBPs) and RanGAP. Here we present the three-dimensional structure of a Ran-RanBP1-RanGAP ternary complex in the ground state and in a transition-state mimic. The structure and biochemical experiments show that RanGAP does not act through an arginine finger, that the basic machinery for fast GTP hydrolysis is provided exclusively by Ran and that correct positioning of the catalytic glutamine is essential for catalysis.
Disease
Known diseases associated with this structure: Osteolysis, familial expansile OMIM:[603499], Paget disease of bone OMIM:[603499]
About this Structure
1K5D is a Protein complex structure of sequences from Homo sapiens and Schizosaccharomyces pombe with and as ligands. Full crystallographic information is available from OCA.
Reference
RanGAP mediates GTP hydrolysis without an arginine finger., Seewald MJ, Korner C, Wittinghofer A, Vetter IR, Nature. 2002 Feb 7;415(6872):662-6. PMID:11832950
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