Conformational alteration of protein synthesis elongation factor EF-Tu by EF-Ts and by kirromycin.
Alterations of the structure of EF-Tu have been investigated by using the rate of EF-Tu cleavage by trypsin as a conformational probe. The presence of EF-Ts bound to EF-Tu results in a 10-fold increase in the cleavage rate. The antibiotic kirromycin, which inhibits protein synthesis by virtue of its interaction with EF-Tu, mimics this effect of EF-Ts. Both kirromycin and EF-Ts also facilitate the exchange of free GDP with GDP bound to EF-Tu. The results suggest that EF-Ts and kirromycin induce a similar conformational change in EF-Tu, thereby "opening" the guanine nucleotide binding site. The trypsin-cleaved EF-Tu still can bind GDP and EF-Ts and can function in Qbeta replicase, but it no longer spontaneously renatures following denaturation in urea.
D000900:Anti-Bacterial Agents; D006153:Guanosine Diphosphate; D007700:Kinetics; D010445:Peptide Elongation Factors; D011487:Protein Conformation; D011489:Protein Denaturation; D011728:Pyridones; D011777:Q beta Replicase; D014357:Trypsin
D000900:Anti-Bacterial Agents; D010445:Peptide Elongation Factors; D011728:Pyridones; D006153:Guanosine Diphosphate; D011777:Q beta Replicase; D014357:Trypsin; C008536:mocimycin
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