1H, 13C and 15N NMR assignments of the E. coli peptide deformylase in complex with a natural inhibitor called actinonin.
In eubacteria, the formyl group of nascent polypeptides is removed by peptide deformylase protein (PDF). This is the reason why PDF has received special attention in the course of the search for new antibacterial agents. We observed by NMR that actinonin, a natural inhibitor, induced drastic changes in the HSQC spectrum of E. coli PDF. We report here the complete NMR chemical shift assignments of PDF resonances bound to actinonin.
Larue
Valéry
V
UMR8015, CNRS, 75006, Paris, France. valery.larue@parisdescartes.fr
Seijo
Bili
B
Tisne
Carine
C
Dardel
Frédéric
F
D000581:Amidohydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002247:Carbon Isotopes / Q000737:chemistry; D006877:Hydroxamic Acids / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons
D002247:Carbon Isotopes; D006877:Hydroxamic Acids; D046912:Multiprotein Complexes; D009587:Nitrogen Isotopes; D021122:Protein Subunits; D011522:Protons; D000581:Amidohydrolases; C084507:peptide deformylase; C010531:actinonin