The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.
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.
Kawashima
T
T
European Molecular Biology Laboratory, Grenoble Outstation, France.
Berthet-Colominas
C
C
Wulff
M
M
Cusack
S
S
Leberman
R
R
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
D010445:Peptide Elongation Factors; C023512:elongation factor Ts; D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu; D008274:Magnesium