| Literature DB >> 26174911 |
Kohei Himeno1, K Johan Rosengren, Tomoko Inoue1, Rodney H Perez1, Michelle L Colgrave, Han Siean Lee, Lai Y Chan, Sónia Troeira Henriques, Koji Fujita1, Naoki Ishibashi1, Takeshi Zendo1, Pongtep Wilaipun2, Jiro Nakayama1, Vichien Leelawatcharamas3, Hiroyuki Jikuya4, David J Craik, Kenji Sonomoto1,4.
Abstract
Enterocin NKR-5-3B, one of the multiple bacteriocins produced by Enterococcus faecium NKR-5-3, is a 64-amino acid novel circular bacteriocin that displays broad-spectrum antimicrobial activity. Here we report the identification, characterization, and three-dimensional nuclear magnetic resonance solution structure determination of enterocin NKR-5-3B. Enterocin NKR-5-3B is characterized by four helical segments that enclose a compact hydrophobic core, which together with its circular backbone impart high stability and structural integrity. We also report the corresponding structural gene, enkB, that encodes an 87-amino acid precursor peptide that undergoes a yet to be described enzymatic processing that involves adjacent cleavage and ligation of Leu(24) and Trp(87) to yield the mature (circular) enterocin NKR-5-3B.Entities:
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Year: 2015 PMID: 26174911 DOI: 10.1021/acs.biochem.5b00196
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162