| Literature DB >> 2682619 |
I Schlichting1, G Rapp, J John, A Wittinghofer, E F Pai, R S Goody.
Abstract
The GTP binding domain of the c-Ha-ras protooncogene product (p21'c) and the corresponding region from an oncogenic mutant form of the protein in which glycine at position 12 has been replaced by valine [p21'(G12V)] have been crystallized with P3-1-(2-nitro)phenylethylguanosine 5'-O-triphosphate (caged GTP) at their active sites. The crystals give x-ray diffraction patterns to a resolution of better than 0.3 nm. Photolysis can be achieved in the crystal, after which GTP hydrolysis takes place at the rate expected from solution studies. Complete x-ray data sets have been obtained for the starting caged-GTP state and the final GDP state after photolysis and hydrolysis, demonstrating the feasibility of time-resolved structural investigations of the process of GTP hydrolysis.Entities:
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Year: 1989 PMID： 2682619 PMCID： PMC298135 DOI： 10.1073/pnas.86.20.7687
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205