Crystal structure of active elongation factor Tu reveals major domain rearrangements
- 1 September 1993
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 365 (6442) , 126-132
- https://doi.org/10.1038/365126a0
Abstract
The crystal structure of intact elongation factor Tu (EF-Tu) from Thermus thermophilus has been determined and refined at an effective resolution of 1.7 Å, with incorporation of data extending to 1.45 Å. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transductlon and amplification of the signal induced by GTP binding as well as for the intrinsic and effector-enhanced GTPase activity of EF-Tu. Comparison of the structure with that of EF-Tu–GDP reveals major mutual rearrange-ments of the three domains of the molecule.Keywords
This publication has 51 references indexed in Scilit:
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- The GTPase superfamily: a conserved switch for diverse cell functionsNature, 1990
- Molecular Switch for Signal Transduction: Structural Differences Between Active and Inactive Forms of Protooncogenic ras ProteinsScience, 1990
- The rate of cleavage of GTP on the binding of Phe-tRNA.elongation factor Tu.GTP to poly(U)-programmed ribosomes of Escherichia coli.Published by Elsevier ,1985
- The accuracy of protein biosynthesis is limited by its speed: high fidelity selection by ribosomes of aminoacyl-tRNA ternary complexes containing GTP[gamma S]Proceedings of the National Academy of Sciences, 1982
- The Antibiotics Kirromycin and Pulvomycin Bind to Different Sites on the Elongation Factor Tu from Esclzerichia coliEuropean Journal of Biochemistry, 1982
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
- Bacteriophage Qβ Replicase Contains the Protein Biosynthesis Elongation Factors EF Tu and EF TsProceedings of the National Academy of Sciences, 1972
- Studies on the purification and properties of factor Tu from E. coliArchives of Biochemistry and Biophysics, 1970
- Separation of three microbial amino acid polymerization factors.Proceedings of the National Academy of Sciences, 1966