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

I Schlichting; S C Almo; G Rapp; K Wilson; K Petratos; A Lentfer; A Wittinghofer; W Kabsch; E F Pai; G A Petsko

doi:10.1038/345309a0

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

Nature. 1990 May 24;345(6273):309-15. doi: 10.1038/345309a0.

Authors

I Schlichting¹, S C Almo, G Rapp, K Wilson, K Petratos, A Lentfer, A Wittinghofer, W Kabsch, E F Pai, G A Petsko, et al.

Affiliation

¹ Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung, Heidelberg, FRG.

PMID: 2111463
DOI: 10.1038/345309a0

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 gamma-phosphate of GTP.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Binding Sites
Chemical Phenomena
Chemistry, Physical
Crystallization
GTP Phosphohydrolases / metabolism
Guanosine Diphosphate / metabolism
Guanosine Triphosphate / metabolism*
Guanylyl Imidodiphosphate / metabolism
Hydrolysis
Lysine
Magnesium / metabolism
Models, Molecular
Molecular Structure
Phosphates / metabolism
Photolysis
Protein Conformation
Proto-Oncogene Proteins / metabolism*
Proto-Oncogene Proteins p21(ras)
X-Ray Diffraction*

Substances

Phosphates
Proto-Oncogene Proteins
Guanosine Diphosphate
Guanylyl Imidodiphosphate
Guanosine Triphosphate
GTP Phosphohydrolases
Proto-Oncogene Proteins p21(ras)
Magnesium
Lysine