title: The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.
abstract: The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dimer, 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.
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, France.
authors.forename: T
authors.initials: T
authors.lastname: Kawashima
authors.forename: C
authors.initials: C
authors.lastname: Berthet-Colominas
authors.forename: M
authors.initials: M
authors.lastname: Wulff
authors.forename: S
authors.initials: S
authors.lastname: Cusack
authors.forename: R
authors.initials: R
authors.lastname: Leberman
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D006153:Guanosine Diphosphate / Q000737:chemistry; D008274:Magnesium / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000737:chemistry*; D010445:Peptide Elongation Factors / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D010445:Peptide Elongation Factors; C023512:elongation factor Ts; D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu; D008274:Magnesium