The structure of the Escherichia coli EF-Tu· EF-Ts complex at 2.5 Å resolution
- 8 February 1996
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 379 (6565), 511-518
- https://doi.org/10.1038/379511a0
Abstract
The crystal structure of the EF-Tu·EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 Å. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dirtier, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.Keywords
This publication has 22 references indexed in Scilit:
- Refined structure of elongation factor EF-Tu from Escherichia coliJournal of Molecular Biology, 1992
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformationNature, 1989
- A simplified procedure for the isolation of bacterial polypeptide elongation factor EF-TuAnalytical Biochemistry, 1980
- Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-Tu, from Escherichia coliJournal of Molecular Biology, 1977
- Bacteriophage Qβ Replicase Contains the Protein Biosynthesis Elongation Factors EF Tu and EF TsProceedings of the National Academy of Sciences of the United States of America, 1972
- Studies on the purification and properties of factor Tu from E. coliArchives of Biochemistry and Biophysics, 1970
- Studies on the role of factor Ts in polypeptide synthesisArchives of Biochemistry and Biophysics, 1970
- Role of GTP in protein synthesis: Interaction of GTP with soluble transfer factors from E. coliArchives of Biochemistry and Biophysics, 1968
- Separation of three microbial amino acid polymerization factors.Proceedings of the National Academy of Sciences of the United States of America, 1966