Essential Role of Histidine 84 in Elongation Factor Tu for the Chemical Step of GTP Hydrolysis on the Ribosome
- 2 September 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 332 (3) , 689-699
- https://doi.org/10.1016/s0022-2836(03)00947-1
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Conformational Change of Elongation Factor Tu (EF-Tu) Induced by Antibiotic BindingJournal of Biological Chemistry, 2001
- Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transferQuarterly Reviews of Biophysics, 1999
- Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E.coli ribosomeThe EMBO Journal, 1998
- Mechanistic Analysis of the Observed Linear Free Energy Relationships in p21ras and Related SystemsBiochemistry, 1996
- Linear Free Energy Relationships in the Intrinsic and GTPase Activating Protein-Stimulated Guanosine 5‘-Triphosphate Hydrolysis of p21rasBiochemistry, 1996
- Regulatory GTPasesCurrent Opinion in Structural Biology, 1995
- Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteinsNature Structural & Molecular Biology, 1995
- Crystal structure of active elongation factor Tu reveals major domain rearrangementsNature, 1993
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- MECHANISM OF ACTION OF KIRROMYCIN-LIKE ANTIBIOTICSAnnual Review of Microbiology, 1985