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

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 th...

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Bibliographic Details
Published in:FEBS letters 1995-01, Vol.357 (3), p.235-238
Main Authors: Metlitskaya, A.Z., Katrukha, G.S., Shashkov, A.S., Zaitsev, D.A., Egorov, Ts.A., Khmel, I.A.
Format: Article
Language:English
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
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(94)01345-2