AI Article Synopsis
- Microcin B17 (McB) is a 43-amino acid antibacterial peptide that targets DNA gyrase and is modified post-translation by the McbBCD synthase.
- The mature form of McB includes eight oxazole and thiazole rings and features a unique backbone ester bond between residues 51 and 52.
- The modification is thought to arise from an N → O shift of the serine residue (Ser(52)), which may be an intermediate in the post-translational processes that create the peptide's heterocycles.
Article Abstract
Microcin B17 (McB) is a 43-amino acid antibacterial peptide targeting the DNA gyrase. The McB precursor is ribosomally produced and then post-translationally modified by the McbBCD synthase. Active mature McB contains eight oxazole and thiazole heterocycles. Here, we show that a major portion of mature McB contains an additional unusual modification, a backbone ester bond connecting McB residues 51 and 52. The modification results from an N → O shift of the Ser(52) residue located immediately downstream of one of McB thiazole heterocycles. We speculate that the N,O-peptidyl shift undergone by Ser(52) is an intermediate of post-translational modification reactions catalyzed by the McbBCD synthase that normally lead to formation of McB heterocycles.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3143593 | PMC |
| http://dx.doi.org/10.1074/jbc.M111.241315 | DOI Listing |
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