Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue

Nature

Volumn 389, Issue 6652, 1997, Pages 758-762

  Rittinger, Katrin ^a   Walker, Philip A ^a   Eccleston, John F ^a   Smerdon, Stephen J ^a   Gamblin, Steven J ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

ARGININE; CDC42 GTP-BINDING PROTEIN; CELL CYCLE PROTEINS; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; GTP PHOSPHOHYDROLASES; GTP-BINDING PROTEINS; GTPASE-ACTIVATING PROTEINS; HYDROGEN BONDING; HYDROLYSIS; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; RHOA GTP-BINDING PROTEIN;

EID: 0030716497     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/39651     Document Type: Article

References (30)

1. Paterson, H. F. et al. Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 111, 1001-1007 (1990).
2. Hall, A. The cellular functions of small GTP-binding proteins. Science 249, 635-640 (1990).
3. Ridley, A. J. & Hall, A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399 (1992).
4. Qiu, R.-G., Chen, J., Kirn, D., McCormick, F. & Symns, M. An essential role for Rac in Ras transformation. Nature 374, 457-459 (1995).
5. Ridley, A. J. Rho: theme and variations. Curr. Biol. 6, 1256-1264 (1996).
6. Coso, O. A. et al. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81, 1137-1146 (1995).
7. Minden, A., Lin, A., Claret, F.-X., Abo, A. & Karin, M. Selective activation of the JNK signaling Cascade and c-Jun Transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81, 1147-1157 (1995).
8. Lancaster, C. et al. Characterization of rhoGAP. J. Biol. Chem. 269, 1137-1142 (1994).
9. Lamarche, N. & Hall, A. GAPs for rho-related GTPases. Trends Genet. 10, 436-440 (1994).
10. Rittinger, K. et al. Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature 388, 693-697 (1997).
11. Wittinghofer, A., Pai, E. & Goody, R. S. Structural and mechanistic aspects of the GTPase reaction of H-ras p21. Handbk Exp. Pharmacol. 108, 195-212 (1993).
12. Barrett, T. et al. The structure of the GTPase-activating domain from p50rhoGAP. Nature 385, 458-461 (1997).
13. Scheffzek, K. et al. The ras-rasGAP complex: Structural basis for GTPase activation and its loss in oncogenic ras mutants. Science 277, 333-338 (1997).
14. iα1 and the mechanism of GTP hydrolysis. Nature 265, 1405-1412 (1994).
15. -. Nature 372, 276-279 (1994).
16. -. Biochemistry 34, 8960-8972 (1995).
17. Schlichting, I. & Reinstein, J. Structures of active conformations of UMP-kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative. Biochemistry 36, 9290-9296 (1997).
18. 3 mimics the transition state of protein phosphorylation in the crystal structure of nucleoside diphosphate and MgADP. Proc. Natl Acad. Sci. USA 94, 3579-3583 (1997).
19. H-ras: An experimental and theoretical study. Biochemistry 33, 3237-3244 (1994).
20. Pai, E. F. et al. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9, 2351-2359 (1990).
21. Hirshberg, M., Stockley, R. W., Dodson, G. & Webb, M. R. The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nature Struct. Biol. 4, 147-152 (1997).
22. Schmidt, G. et al. Gln63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature 387, 725-729 (1997).
23. Rho by deamidation of glutamine. Nature 387, 729-733 (1997).
24. Maegley, K. A., Admiral, S. J. & Herschlag, D. Ras-catalysed hydrolysis of GTP: A new perspective from model studies. Proc. Natl Acad. Sci. USA 93, 8160-8166 (1996).
25. McCormick, F. Gasp: not just another oncogene. Nature 340, 678-679 (1989).
26. iα1: Stabilisation of the transition state for GTP hydrolysis. Cell 89, 251-261 (1997).
27. Bernstein, B. E., Michels, P. A. M. & Hol, W. G. J. Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. Nature 385, 275-278 (1997).
28. CCP4. The CCP4 suite: programs for X-ray crystallography. Acta Crystallogr. D 50, 760-763 (1994).
29. Carson, M. Ribbons 2.0. J. Appl. Crystallogr. 24, 958-961 (1991).
30. Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).