The molecular basis of kirromycin (mocimycin) action; a 1H NMR study using deuterated elongation factor Tu.
The binding of the antibiotic kirromycin (mocimycin) to its target protein, bacterial elongation factor Tu (EF-Tu), has been studied by 1H NMR spectroscopy using deuterated protein. Narrow lines were observed in the spectrum of the unbound protein (due to residual protons) and in the spectrum of the kirromycin-EF-Tu complex. The spectrum of the complex has been compared with the spectra of the unbound protein and the unbound drug, and the results are interpreted in terms of the mode of antibiotic action of kirromycin.
Barber
J
J
Department of Pharmacy, University of Manchester, UK.
Carver
J A
JA
Leberman
R
R
Tebb
G M
GM
D003903:Deuterium; D009682:Magnetic Resonance Spectroscopy; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D011485:Protein Binding; D011728:Pyridones / Q000493:pharmacokinetics
D011728:Pyridones; D003903:Deuterium; D010444:Peptide Elongation Factor Tu; C008536:mocimycin