A common structural motif in elongation factor Ts and ribosomal protein L7/12 may be involved in the interaction with elongation factor Tu.
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 alpha A--beta D--alpha B 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.
Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany.
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Wieden
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Wintermeyer
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Rodnina
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D001665:Binding Sites; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000235:genetics / Q000378:metabolism*; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment
D001426:Bacterial Proteins; D010445:Peptide Elongation Factors; D012269:Ribosomal Proteins; C023512:elongation factor Ts; C016700:ribosomal protein L7-L12; D010444:Peptide Elongation Factor Tu