1gil

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{{STRUCTURE_1gil| PDB=1gil | SCENE= }}
{{STRUCTURE_1gil| PDB=1gil | SCENE= }}
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'''STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS'''
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===STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8073283 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8073283}}
==About this Structure==
==About this Structure==
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[[Category: Sprang, S R.]]
[[Category: Sprang, S R.]]
[[Category: Gtp-binding protein]]
[[Category: Gtp-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:21:05 2008''

Revision as of 02:21, 1 July 2008

Image:1gil.png

Template:STRUCTURE 1gil

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

Template:ABSTRACT PUBMED 8073283

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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