Download MendeleyThe pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins.
Scheidig, A.J., Burmester, C., Goody, R.S.(1999) Structure 7: 1311-1324
- PubMed: 10574788
- DOI: https://doi.org/10.1016/s0969-2126(00)80021-0
- Primary Citation of Related Structures:
1CTQ, 1QRA - PubMed Abstract:
In numerous biological events the hydrolysis of guanine triphosphate (GTP) is a trigger to switch from the active to the inactive protein form. In spite of the availability of several high-resolution crystal structures, the details of the mechanism of nucleotide hydrolysis by GTPases are still unclear. This is partly because the structures of the proteins in their active states had to be determined in the presence of non-hydrolyzable GTP analogues (e.g. GppNHp). Knowledge of the structure of the true Michaelis complex might provide additional insights into the intrinsic protein hydrolysis mechanism of GTP and related nucleotides.
Organizational Affiliation:
Abteilung für Physikalische Biochemie, Max-Planck Institute for Molecular Physiology, Dortmund, 44227, Germany. scheidig@mpi-dortmund.mpg.de
