期刊
JOURNAL OF MOLECULAR EVOLUTION
卷 52, 期 2, 页码 129-136出版社
SPRINGER
DOI: 10.1007/s002390010141
关键词
protein synthesis; nucleotide exchange; translation; ribosomal proteins
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 alphaA-betaD-alphaB 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.
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