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This article is missing information about Microcin B17 and sagBCD family. Please expand the article to include this information. Further details may exist on the talk page.(December 2020)
Stainless steel sculpture based on the structure of the protein microcin J25. Author: Julian Voss-Andreae
Microcins are very small bacteriocins, composed of relatively few amino acids. For this reason, they are distinct from their larger protein cousins. The classic example is microcin V, of Escherichia coli. Subtilosin A is another bacteriocin from Bacillus subtilis. The peptide has a cyclized backbone and forms three cross-links between the sulphurs of Cys13, Cys7 and Cys4 and the alpha-positions of Phe22, Thr28 and Phe31.[1]
Microcins produced by commensalE. coli strains target and eliminate enteric pathogens such as Salmonella enterica by mimicking the siderophores the pathogens use for iron scavenging.[2] Microcins also help commensal strains of E. coli outcompete pathogenic strains.[3]
BACTIBASE[4][5] database is an open-access database for bacteriocins including microcins.
References
↑Kawulka KE, Sprules T, Diaper CM, Whittal RM, McKay RT, Mercier P, Zuber P, Vederas JC (March 2004). "Structure of subtilosin A, a cyclic antimicrobial peptide from Bacillus subtilis with unusual sulfur to alpha-carbon cross-links: formation and reduction of alpha-thio-alpha-amino acid derivatives". Biochemistry. 43 (12): 3385–95. doi:10.1021/bi0359527. PMID15035610.
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