The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
Abstract
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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Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
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Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543
Classification and evolution of P-loop GTPases and related ATPases
Leipe, D. D., Wolf, Y. I., Koonin, E. V., & Aravind, L. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5378 · Cited by 1,148
Regulation, signaling, and physiological functions of G-Proteins
Syrovatkina, V., Alegre, K. O., Dey, R., & Huang, X.-Y. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.002 · Cited by 498
GTPase-activating proteins: Helping hands to complement an active site
Scheffzek, K., Ahmadian, M. R., & Wittinghofer, A. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01224-9 · Cited by 410
A Spectroscopic Mechanism for Primary Olfactory Reception
Turin, L. (1996) · Chemical Senses · doi:10.1093/chemse/21.6.773 · Cited by 388
Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP
Rittinger, K., Walker, P. A., Eccleston, J. F., Nurmahomed, K., Owen, D., Laue, E., Gamblin, S. J., & Smerdon, S. J. (1997) · Nature · doi:10.1038/41805 · Cited by 227
Crystal Structure of Human RhoA in a Dominantly Active Form Complexed with a GTP Analogue
Ihara, K., Muraguchi, S., Kato, M., Shimizu, T., Shirakawa, M., Kuroda, S., Kaibuchi, K., & Hakoshima, T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9656 · Cited by 190
Modulation of Host Signaling by a Bacterial Mimic
Stebbins, C. E., & Galán, J. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00141-6 · Cited by 160
The interaction of Ras with GTPase‐activating proteins
Wittinghofer, A., Scheffzek, K., & Ahmadian, M. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00321-9 · Cited by 135
Preininger, A. M., Meiler, J., & Hamm, H. E. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.04.011 · Cited by 104
Fonin, A. V., Darling, A. L., Kuznetsova, I. M., Turoverov, K. K., & Uversky, V. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03276-1 · Cited by 91
Jeong, J.-H., Lee, K.-H., Kim, Y.-M., Kim, D.-H., Oh, B.-H., & Kim, Y.-G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c112.384420 · Cited by 68
“Analogously, in the structure of the heterotrimeric GTPase subunit Gt , the side chain of Arg174 in the switch I region stabilizes the transition state of the -phosphate (19).”
BackgroundStructural model for differential cap maturation at growing microtubule ends
Estévez-Gallego, J., Josa-Prado, F., Ku, S., Buey, R. M., Balaguer, F. A., Prota, A. E., Lucena-Agell, D., Kamma-Lorger, C., Yagi, T., Iwamoto, H., et al. (2020) · eLife · doi:10.7554/elife.50155 · Cited by 65
Deprotonation of Water in the Presence of Carboxylate and Magnesium Ions
Katz, A. K., Glusker, J. P., Markham, G. D., & Bock, C. W. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp9815412 · Cited by 56
Structural Evidence for a Sequential Release Mechanism for Activation of Heterotrimeric G Proteins
Kapoor, N., Menon, S. T., Chauhan, R., Sachdev, P., & Sakmar, T. P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.08.043 · Cited by 47
Francis, B. R. (2013) · Journal of Molecular Evolution · doi:10.1007/s00239-013-9567-y · Cited by 34
Mechanism of Regulation of Prokaryotic Tubulin-like GTPase FtsZ by Membrane Protein EzrA
Chung, K.-M., Hsu, H.-H., Yeh, H.-Y., & Chang, B.-Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m605177200 · Cited by 32
PA binding of phosphatidylinositol 4-phosphate 5-kinase
Stace, C., Manifava, M., Delon, C., Coadwell, J., Cockcroft, S., & Ktistakis, N. T. (2008) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2007.11.008 · Cited by 30
Metadata
- Authors
- Coleman, D., Berghuis, A., Lee, E., Linder, M., Gilman, A., & Sprang
- Venue
- Science
- Published
- 1994-09-02
- Volume
- 265
- Issue
- 5177
- Pages
- 1405-1412
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2022754746
- Cited by
- 825
- References
- 2
- FWCI
- 24.63
- Type
- journal article
- Language
- en
- Open access
- closed
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