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Science 2 September 1994:
Vol. 265. no. 5177, pp. 1405 - 1412
DOI: 10.1126/science.8073283
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Articles

Science, Vol 265, Issue 5177, 1405-1412
Copyright © 1994 by American Association for the Advancement of Science

articles

Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis

DE Coleman, AM Berghuis, E Lee, ME Linder, AG Gilman, and Sprang SR

Howard Hughes Medical Institute, Dallas, TX.

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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J. Biol. Chem. 273, 6731-6735
   Abstract »    Full Text »    PDF »
Genetic Selection of Mammalian Adenylyl Cyclases Insensitive to Stimulation by Gsalpha.
G. Zimmermann, D. Zhou, and R. Taussig (1998)
J. Biol. Chem. 273, 6968-6975
   Abstract »    Full Text »    PDF »
Selective Uncoupling of RGS Action by a Single Point Mutation in the G Protein alpha -Subunit.
P. R. DiBello, T. R. Garrison, D. M. Apanovitch, G. Hoffman, D. J. Shuey, K. Mason, M. I. Cockett, and H. G. Dohlman (1998)
J. Biol. Chem. 273, 5780-5784
   Abstract »    Full Text »    PDF »
alpha Helix Content of G Protein alpha  Subunit Is Decreased upon Activation by Receptor Mimetics.
T. Tanaka, T. Kohno, S.'i. Kinoshita, H. Mukai, H. Itoh, M. Ohya, T. Miyazawa, T. Higashijima, and K. Wakamatsu (1998)
J. Biol. Chem. 273, 3247-3252
   Abstract »    Full Text »    PDF »
Mammalian RGS Proteins: Barbarians at the Gate.
D. M. Berman and A. G. Gilman (1998)
J. Biol. Chem. 273, 1269-1272
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Mechanism of RGS4, a GTPase-activating Protein for G Protein alpha  Subunits.
S. P. Srinivasa, N. Watson, M. C. Overton, and K. J. Blumer (1998)
J. Biol. Chem. 273, 1529-1533
   Abstract »    Full Text »    PDF »
The Bacterial Enhancer-binding Protein NtrC as a Molecular Machine.
I. ROMBEL, A. NORTH, I. HWANG, C. WYMAN, and S. KUSTU (1998)
Cold Spring Harb Symp Quant Biol 63, 157-166
   Abstract »    PDF »
Molecular Determinants of Selectivity in 5-Hydroxytryptamine1B Receptor-G Protein Interactions.
H. Bae, K. Anderson, L. A. Flood, N. P. Skiba, H. E. Hamm, and S. G. Graber (1997)
J. Biol. Chem. 272, 32071-32077
   Abstract »    Full Text »    PDF »
Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in a Complex with Gsalpha ·GTPgamma S.
J. J. Tesmer, R. K. Sunahara, A. G. Gilman, and S. R. Sprang (1997)
Science 278, 1907-1916
   Abstract »    Full Text »
Crystal Structure of the Adenylyl Cyclase Activator Gsalpha .
R. K. Sunahara, J. J. Tesmer, A. G. Gilman, and S. R. Sprang (1997)
Science 278, 1943-1947
   Abstract »    Full Text »
Catalytic mechanism of the adenylyl and guanylyl cyclases: Modeling and mutational analysis.
Y. Liu, A. E. Ruoho, V. D. Rao, and J. H. Hurley (1997)
PNAS 94, 13414-13419
   Abstract »    Full Text »    PDF »
Inhibition of regulator of G protein signaling function by two mutant RGS4 proteins.
K. M. Druey and J. H. Kehrl (1997)
PNAS 94, 12851-12856
   Abstract »    Full Text »    PDF »


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