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.

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