Identification, Characterization, and Three-Dimensional Structure of the Novel Circular Bacteriocin, Enterocin NKR-5-3B, from Enterococcus faecium

Himeno, Kohei, Rosengren, K. Johan, Inoue, Tomoko, Perez, Rodney H., Colgrave, Michelle L., Lee, Han Siean, Chan, Lai Y., Henriques, Sonia Troeira, Fujita, Koji, Ishibashi, Naoki, Zendo, Takeshi, Wilaipun, Pongtep, Nakayama, Jiro, Leelawatcharamas, Vichien, Jikuya, Hiroyuki, Craik, David J. and Sonomoto, Kenji (2015) Identification, Characterization, and Three-Dimensional Structure of the Novel Circular Bacteriocin, Enterocin NKR-5-3B, from Enterococcus faecium. Biochemistry, 54 31: 4863-4876. doi:10.1021/acs.biochem.5b00196


Author Himeno, Kohei
Rosengren, K. Johan
Inoue, Tomoko
Perez, Rodney H.
Colgrave, Michelle L.
Lee, Han Siean
Chan, Lai Y.
Henriques, Sonia Troeira
Fujita, Koji
Ishibashi, Naoki
Zendo, Takeshi
Wilaipun, Pongtep
Nakayama, Jiro
Leelawatcharamas, Vichien
Jikuya, Hiroyuki
Craik, David J.
Sonomoto, Kenji
Title Identification, Characterization, and Three-Dimensional Structure of the Novel Circular Bacteriocin, Enterocin NKR-5-3B, from Enterococcus faecium
Journal name Biochemistry   Check publisher's open access policy
ISSN 0006-2960
1520-4995
Publication date 2015-08-11
Year available 2015
Sub-type Article (original research)
DOI 10.1021/acs.biochem.5b00196
Open Access Status Not Open Access
Volume 54
Issue 31
Start page 4863
End page 4876
Total pages 14
Place of publication Washington, DC United States
Publisher American Chemical Society
Collection year 2016
Language eng
Formatted 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 Leu24 and Trp87 to yield the mature (circular) enterocin NKR-5-3B.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 4 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 4 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 25 Aug 2015, 00:19:31 EST by System User on behalf of Institute for Molecular Bioscience