1gil: Difference between revisions

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[[Image:1gil.jpg|left|200px]]
[[Image:1gil.jpg|left|200px]]


{{Structure
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|LIGAND= <scene name='pdbligand=GSP:5&#39;-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gil OCA], [http://www.ebi.ac.uk/pdbsum/1gil PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gil RCSB]</span>
}}


'''STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS'''
'''STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS'''
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[[Category: Coleman, D E.]]
[[Category: Coleman, D E.]]
[[Category: Sprang, S R.]]
[[Category: Sprang, S R.]]
[[Category: gtp-binding protein]]
[[Category: Gtp-binding protein]]
 
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Revision as of 17:37, 2 May 2008

File:1gil.jpg

Template:STRUCTURE 1gil

STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS


OverviewOverview

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 StructureAbout this Structure

1GIL is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 17:37:10 2008

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