Microcins
Oxford Dictionary of Biochemistry:
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microcin
any of a number of microbial peptide toxins that have antibiotic action. They are of diverse structure and action. Examples include microcin E492, a 6 kDa polypeptide antibiotic. It forms cation-selective channels in planar phospholipid bilayers, leading to a loss of membrane potential. Another example is microcin B17 from E. coli. This is a glycine-rich peptide that inhibits DNA gyrase (see (DNA) topoisomerase type II). Microcin is classified in the TC system under number 1.C.58.
| microchemistry, microcell, microcarrier | |
| micrococcal, microconcentrator, microcrystal |
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Microcins
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| structure of subtilosin a | |||||||||
| Identifiers | |||||||||
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| Symbol | Subtilosin_A | ||||||||
| Pfam | PF11420 | ||||||||
| InterPro | IPR021539 | ||||||||
| TCDB | 9.A.52 | ||||||||
| OPM family | 164 | ||||||||
| OPM protein | 1q71 | ||||||||
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Microcins are very small bacteriocins, composed of a relatively few peptides. For this reason, they are distinct from their larger protein cousins. The classic example is microcin V, of E. coli. Subtilosin A is another bacteriocin from Bacillus subtilis. The peptide has a cyclized backbone and forms three cross-liks between the sulphurs of Cys13, Cys7 and Cys4 and the alpha-positions of Phe22,Thr28 and Phe31.[1]
BACTIBASE[2][3] database is an open-access database for bacteriocins including microcins (view complete list).
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. PMID 15035610.
- ^ Hammami R, Zouhir A, Ben Hamida J, Fliss I (2007). "BACTIBASE: a new web-accessible database for bacteriocin characterization". BMC Microbiology 7: 89. doi:10.1186/1471-2180-7-89. PMC 2211298. PMID 17941971. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2211298.
- ^ Hammami R, Zouhir A, Le Lay C, Ben Hamida J, Fliss I (2010). "BACTIBASE second release: a database and tool platform for bacteriocin characterization.". BMC Microbiology 10: 22. doi:10.1186/1471-2180-10-22. PMC 2824694. PMID 20105292. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2824694.
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