Overexpression, purification, crystallization and preliminary X-ray diffraction of the nisin resistance protein from Streptococcus agalactiae

被引:5
|
作者
Khosa, Sakshi [1 ]
Hoeppner, Astrid [2 ]
Kleinschrodt, Diana [3 ]
Smits, Sander H. J. [1 ]
机构
[1] Univ Dusseldorf, Inst Biochem, D-40225 Dusseldorf, Germany
[2] Univ Dusseldorf, Crystal Farm & Xray Facil, D-40225 Dusseldorf, Germany
[3] Univ Dusseldorf, Prot Prod Facil, D-40225 Dusseldorf, Germany
关键词
lantibiotic; nisin; resistance; immunity; lipoprotein; Lactococcus lactis; BIOSYNTHESIS; LANTIBIOTICS; MODE;
D O I
10.1107/S2053230X15006226
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Nisin is a 34-amino-acid antimicrobial peptide produced by Lactococcus lactis belonging to the class of lantibiotics. Nisin displays a high bactericidal activity against various Gram-positive bacteria, including some human-pathogenic strains. However, there are some nisin-non-producing strains that are naturally resistant owing to the presence of the nsr gene within their genome. The encoded protein, NSR, cleaves off the last six amino acids of nisin, thereby reducing its bactericidal efficacy. An expression and purification protocol has been established for the NSR protein from Streptococcus agalactiae COH1. The protein was successfully crystallized using the vapour-diffusion method in hanging and sitting drops, resulting in crystals that diffracted X-rays to 2.8 and 2.2 angstrom, respectively.
引用
收藏
页码:671 / 675
页数:5
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