Abstract.
Elongation factor (EF) Tu alternates between two interaction partners, EF-Ts and the ribosome, during its functional cycle. On the ribosome, the interaction involves, among others, ribosomal protein L7/12. Here we compare EF-Ts and L7/12 with respect to the conservation of sequence and structure. There is significant conservation of functionally important residues in the N-terminal domain of EF-Ts and in the C-terminal domain of L7/12. The structure alignment based on the crystal structures of the two domains suggests a high degree of similarity between the αA–βD–αB motif in L7/12 and the h1–turn–h2 motif in EF-Ts which defines a common structural motif. The motif is remarkably similar with respect to fold, bulkiness, and charge distribution of the solution surface, suggesting that it has a common function in binding EF-Tu.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
Author information
Authors and Affiliations
Additional information
Received: 12 June 2000 / Accepted: 10 October 2000
Rights and permissions
About this article
Cite this article
Wieden, HJ., Wintermeyer, W. & Rodnina, M. A Common Structural Motif in Elongation Factor Ts and Ribosomal Protein L7/12 May Be Involved in the Interaction with Elongation Factor Tu. J Mol Evol 52, 129–136 (2001). https://doi.org/10.1007/s002390010141
Issue Date:
DOI: https://doi.org/10.1007/s002390010141