Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

Ilme Schlichting, Steven C. Almo, Gert Rapp, Keith Wilson, Kyriakos Petratos, Arno Lentfer, Alfred Wittinghofer, Wolfgang Kabsch, Emil F. Pai, Gregory A. Petsko, Roger S. Goody

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398 Scopus citations

Abstract

Crystals of Ha-Ras p21 with caged GTP at the active site have been used to investigate the conformational changes of p21 on GTP hydrolysis. The structure of the short-lived p21-GTP complex was determined by Laue diffraction methods. After GTP hydrolysis, substantial structural changes occur in the parts of the molecule implicated in the interaction with GTPase-activating protein. The trigger for this process seems to be a change in coordination of the active-site Mg2+ion as a result of loss of the γ-phosphate of GTP.

Original languageEnglish (US)
Pages (from-to)309-315
Number of pages7
JournalNature
Volume345
Issue number6273
DOIs
StatePublished - Jan 1 1990
Externally publishedYes

ASJC Scopus subject areas

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    Schlichting, I., Almo, S. C., Rapp, G., Wilson, K., Petratos, K., Lentfer, A., Wittinghofer, A., Kabsch, W., Pai, E. F., Petsko, G. A., & Goody, R. S. (1990). Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis. Nature, 345(6273), 309-315. https://doi.org/10.1038/345309a0