The structure of the lantibiotic lacticin 481 produced by Lactococcus lactis: Location of the thioether bridges

被引:50
作者
vandenHooven, HW
Lagerwerf, FM
Heerma, W
Haverkamp, J
Piard, JC
Hilbers, CW
Siezen, RJ
Kuipers, OP
Rollema, HS
机构
[1] UNIV UTRECHT, BIJVOET CTR BIOMOL RES, MASS SPECTROMETRY GRP, NL-3508 TB UTRECHT, NETHERLANDS
[2] CATHOLIC UNIV NIJMEGEN, NSR, CTR MOL STRUCT DESIGN & SYNTH, LAB BIOPHYS CHEM, NL-6525 ED NIJMEGEN, NETHERLANDS
来源
FEBS LETTERS | 1996年 / 391卷 / 03期
关键词
bacteriocin; lanthionine-containing polypeptide; post-translational modification; cyanogen bromide cleavage; NMR; mass spectrometry;
D O I
10.1016/0014-5793(96)00771-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The lantibiotic lacticin 481 is a bacteriocin produced by Lactococcus lactis ssp, lactis, This polypeptide contains 27 amino acids, including the unusual residues dehydrobutyrine and the thioether-bridging lanthionine and 3-methyllanthionine. Lacticin 481 belongs to a structurally distinct group of lantibiotics, which also include streptococcin A-FF22, salivaricin A and variacin, Here we report the first complete structure of this type of lantibiotic. The exact location of the thioether bridges in lacticin 481 was determined by a combination of peptide chemistry, mass spectrometry and NMR spectroscopy, showing connections between residues 9 and 14, 11 and 25, and 18 and 26.
引用
收藏
页码:317 / 322
页数:6
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