Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure.

@article{Duisterwinkel1984SpecificAO,
  title={Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure.},
  author={F. J. Duisterwinkel and Barend Kraal and Jochum De Graaf and Adriaan Talens and Leendert Bosch and G W Swart and Andrea Parmeggiani and T F la Cour and Jens Nyborg and Brian F. C. Clark},
  journal={The EMBO journal},
  year={1984},
  volume={3 1},
  pages={113-20}
}
Specific alterations of the elongation factor Tu (EF-Tu) polypeptide chain have been identified in a number of mutant species of this elongation factor. In two species, Ala-375, located on domain II, was found by amino acid analysis to be replaced by Thr and Val, respectively. These replacements substantially lower the affinity of EF-Tu.GDP for the antibiotic kirromycin. Since kirromycin can be cross-linked to Lys-357, also located on domain II but structurally very far from Ala-375, these data… CONTINUE READING