Structure of microcin C51, a new antibiotic with a broad spectrum of activity

• Published in: FEBS letters Vol. 357; no. 3; pp. 235 - 238
• Main Authors: Metlitskaya, A.Z., Katrukha, G.S., Shashkov, A.S., Zaitsev, D.A., Egorov, Ts.A., Khmel, I.A.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 09.01.1995
• Subjects: acetic acid; ACOH; Amino Acid Sequence; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - pharmacology; Bacteriocins - chemistry; Bacteriocins - pharmacology; correlation spectroscopy; COSY; Escherichia coli; heteronuclear multiple quantum coherence; HQMC; Magnetic Resonance Spectroscopy; Mcc; Microcin; Molecular Sequence Data; NMR; nuclear magnetic resonance; Nucleotide peptide; one dimensional; open reading frame; ORF; parts per million; Peptide antibiotic; ppm; Protein Conformation; TFA; trifluoroacetic acid; two dimensional; ORF; Peptide antibiotic; ACOH; Mcc; ppm; COSY; TFA; 2D; NMR; 1D; Nucleotide peptide; Microcin; HQMC
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(94)01345-2

The structure of microcin C51, a new antibiotic produced by E. coli, has been determined. This antibiotic was shown to be a 1.18 kDa nucleotide peptide. It consists of a heptapeptide with formylmethionine as the N-terminus and a C-terminal asparagine linked with nebularin-5′-monophosphate through the three-methylene bridge. The OH-group of threonine is substituted. The peptide chain of microcin C51 synthesized on ribosomes is the longest among the known biologically active nucleotide peptides.