1gil: Difference between revisions

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{{STRUCTURE_1gil|  PDB=1gil  |  SCENE=  }}  
{{STRUCTURE_1gil|  PDB=1gil  |  SCENE=  }}  


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




==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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{{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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