Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot.
نویسندگان
چکیده
The antibacterial peptide microcin J25 (MccJ25) inhibits bacterial transcription by binding within, and obstructing, the nucleotide-uptake channel of bacterial RNA polymerase. Published covalent and three-dimensional structures indicate that MccJ25 is a 21-residue cycle. Here, we show that the published covalent and three-dimensional structures are incorrect, and that MccJ25 in fact is a 21-residue "lariat protoknot", consisting of an 8-residue cyclic segment followed by a 13-residue linear segment that loops back and threads through the cyclic segment. MccJ25 is the first example of a lariat protoknot involving a backbone-side chain amide linkage.
منابع مشابه
Synthesis of a peptide derivative of microcin J25 and evaluation of antibacterial and biological activities
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Microcin J25 (MccJ25) is a small ribosomally synthesized antimicrobial peptide that is produced by Enterobacteriacea family especially E.coli. The present study focuses on preparation and evaluation of in vitro antimicrobial and biological properties of a new peptide derived from MccJ25. We prepared a MccJ25-derived peptide containing 14 amino acids and a single intra-molecular disulfide bond a...
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عنوان ژورنال:
- Journal of the American Chemical Society
دوره 125 41 شماره
صفحات -
تاریخ انتشار 2003