1srq
From Proteopedia
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| - | [[Image:1srq.gif|left|200px]] | + | [[Image:1srq.gif|left|200px]] |
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| - | '''Crystal Structure of the Rap1GAP catalytic domain''' | + | {{Structure |
| + | |PDB= 1srq |SIZE=350|CAPTION= <scene name='initialview01'>1srq</scene>, resolution 2.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= RAP1GA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of the Rap1GAP catalytic domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SRQ is a [ | + | 1SRQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRQ OCA]. |
==Reference== | ==Reference== | ||
| - | The GTPase-activating protein Rap1GAP uses a catalytic asparagine., Daumke O, Weyand M, Chakrabarti PP, Vetter IR, Wittinghofer A, Nature. 2004 May 13;429(6988):197-201. PMID:[http:// | + | The GTPase-activating protein Rap1GAP uses a catalytic asparagine., Daumke O, Weyand M, Chakrabarti PP, Vetter IR, Wittinghofer A, Nature. 2004 May 13;429(6988):197-201. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15141215 15141215] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: mixed alpha-beta]] | [[Category: mixed alpha-beta]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:08:49 2008'' |
Revision as of 12:08, 20 March 2008
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| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | RAP1GA1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Rap1GAP catalytic domain
Overview
Rap1 is a Ras-like guanine-nucleotide-binding protein (GNBP) that is involved in a variety of signal-transduction processes. It regulates integrin-mediated cell adhesion and might activate extracellular signal-regulated kinase. Like other Ras-like GNBPs, Rap1 is regulated by guanine-nucleotide-exchange factors (GEFs) and GTPase-activating proteins (GAPs). These GAPs increase the slow intrinsic GTPase reaction of Ras-like GNBPs by many orders of magnitude and allow tight regulation of signalling. The activation mechanism involves stabilization of the catalytic glutamine of the GNBP and, in most cases, the insertion of a catalytic arginine of GAP into the active site. Rap1 is a close homologue of Ras but does not possess the catalytic glutamine essential for GTP hydrolysis in all other Ras-like and Galpha proteins. Furthermore, RapGAPs are not related to other GAPs and apparently do not use a catalytic arginine residue. Here we present the crystal structure of the catalytic domain of the Rap1-specific Rap1GAP at 2.9 A. By mutational analysis, fluorescence titration and stopped-flow kinetic assay, we demonstrate that Rap1GAP provides a catalytic asparagine to stimulate GTP hydrolysis. Implications for the disease tuberous sclerosis are discussed.
About this Structure
1SRQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The GTPase-activating protein Rap1GAP uses a catalytic asparagine., Daumke O, Weyand M, Chakrabarti PP, Vetter IR, Wittinghofer A, Nature. 2004 May 13;429(6988):197-201. PMID:15141215
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