Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli.
Microcin 7 is a small peptide produced and excreted to the culture medium by stationary-phase Escherichia coli cells harboring the pMccC7 plasmid (formerly named pRYC7). This peptide inhibited the growth of the enterobacteria phylogenetically closer to E. coli, apparently by blocking protein biosynthesis. The molecule was degraded with trypsin, and the resulting fragments were purified and sequenced. The results show that microcin 7 is a linear heptapeptide blocked at both ends.
Garcia-Bustos
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JF
Pezzi
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Mendez
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D000215:Acylation; D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000032:analysis / Q000494:pharmacology*; D001430:Bacteriocins; D018826:CD13 Antigens; D002268:Carboxypeptidases / Q000378:metabolism; D043422:Carboxypeptidases A; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000378:metabolism*; D006868:Hydrolysis; D007930:Leucine / Q000378:metabolism; D010455:Peptides / Q000032:analysis / Q000494:pharmacology*; D013997:Time Factors; D014357:Trypsin
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D010455:Peptides; C020411:microcin; D002268:Carboxypeptidases; D000626:Aminopeptidases; D018826:CD13 Antigens; D043422:Carboxypeptidases A; D014357:Trypsin; D007930:Leucine