Affinity with which EF-Tu binds to aa-tRNA in its GTP-bound active state

Range ≈1e-8 M
Organism bacteria
Reference Boltaña S, Reyes-Lopez F, Morera D, Goetz F, MacKenzie SA. Divergent responses to peptidoglycans derived from different E. coli serotypes influence inflammatory outcome in trout, Oncorhynchus mykiss, macrophages. BMC Genomics. 2011 Jan 14 12: 34. doi: 10.1186/1471-2164-12-34. p.684 left columnPubMed ID21235753
Primary Source A. Pingoud, F.-U. Gast, W. Block, F. Peters, The elongation factor Tu from Escherichia coli , aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is bound by programmed ribosomes, J. Biol. Chem. 258 (1983) 14200 – 14205.PubMed ID6358217
Comments "EF-Tu participates in the cyclic process of mRNA-directed polypeptide synthesis through the delivery of aminoacyl-tRNA (aa-tRNA) to the A-site of actively translating ribosomes. In its GTP-bound active state, EF-Tu binds to aa-tRNA with high affinity (KD˜10^-8M)[primary source], forming an EF-Tu•GTP•aa-tRNA ternary complex [ref 4]."
Entered by Uri M
ID 110161