1gil
From Proteopedia
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| - | [[Image:1gil.jpg|left|200px]] | + | [[Image:1gil.jpg|left|200px]] |
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| - | '''STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS''' | + | {{Structure |
| + | |PDB= 1gil |SIZE=350|CAPTION= <scene name='initialview01'>1gil</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GSP:5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GIL is a [ | + | 1GIL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GIL OCA]. |
==Reference== | ==Reference== | ||
| - | Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis., Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR, Science. 1994 Sep 2;265(5177):1405-12. PMID:[http:// | + | Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis., Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR, Science. 1994 Sep 2;265(5177):1405-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8073283 8073283] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gtp-binding protein]] | [[Category: gtp-binding protein]] | ||
| - | ''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 11:23:36 2008'' |
Revision as of 09:23, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS
Overview
Mechanisms of guanosine triphosphate (GTP) hydrolysis by members of the G protein alpha subunit-p21ras superfamily of guanosine triphosphatases have been studied extensively but have not been well understood. High-resolution x-ray structures of the GTP gamma S and GDP.AlF4- complexes formed by the G protein Gi alpha 1 demonstrate specific roles in transition-state stabilization for two highly conserved residues. Glutamine204 (Gln61 in p21ras) stabilizes and orients the hydrolytic water in the trigonal-bipyramidal transition state. Arginine 178 stabilizes the negative charge at the equatorial oxygen atoms of the pentacoordinate phosphate intermediate. Conserved only in the G alpha family, this residue may account for the higher hydrolytic rate of G alpha proteins relative to those of the p21ras family members. The fold of Gi alpha 1 differs from that of the homologous Gt alpha subunit in the conformation of a helix-loop sequence located in the alpha-helical domain that is characteristic of these proteins; this site may participate in effector binding. The amino-terminal 33 residues are disordered in GTP gamma S-Gi alpha 1, suggesting a mechanism that may promote release of the beta gamma subunit complex when the alpha subunit is activated by GTP.
About this Structure
1GIL is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis., Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR, Science. 1994 Sep 2;265(5177):1405-12. PMID:8073283
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