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PMID: 2111463 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Nature ·Vol. 345 ·No. 6273 ·1990-05-24 ·Pages 309-15

Schlichting I, Almo SC, Rapp G, Wilson K, Petratos K, Lentfer A, Wittinghofer A, Kabsch W, Pai EF, Petsko GA

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.

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
Chemicals
Phosphates Proto-Oncogene Proteins Guanosine Diphosphate Guanylyl Imidodiphosphate Guanosine Triphosphate GTP Phosphohydrolases Proto-Oncogene Proteins p21(ras) Magnesium Lysine
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Schlichting I
Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung, Heidelberg, FRG.
Almo S C
Rapp G
Wilson K
Petratos K
Lentfer A
Wittinghofer A
Kabsch W
Pai E F
Petsko G A
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
DOI
10.1038/345309a0
Published
1990-05-24
Pages
309-15
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
PMID: 2188134
External Links
PubMed source DOI: 10.1038/345309a0 View journal details
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