Mutant species of EF-Tu, altered at position 375, exhibit a reduced affinity for aminoacylated transfer-RNAs.
The interaction between EF-Tu X GTP and aminoacyl-tRNA is shown to be influenced by mutations at site 375 of this three-domain protein. Site 375 is located in domain II near the interface with domain I [(1984) EMBO J. 3, 113-120]. Replacement of the alanine at this site by a threonine or valine residue results in lower binding constants with Phe-tRNA and Tyr-tRNA, as was evaluated by the hydrolysis protection technique. The data are discussed in the light of what is known about the three-dimensional structure of the protein and its interaction sites with aminoacyl-tRNA.
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000032:analysis / Q000235:genetics; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D009154:Mutation; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000235:genetics / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D013329:Structure-Activity Relationship
D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu