Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis

被引：260

作者：

Li, B

Yu, JPJ

Brunzelle, JS

Moll, GN

van der Donk, WA

Nair, SK

机构：

[1] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

[2] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

[3] Univ Illinois, Ctr Biophys & Computat Biol, Urbana, IL 61801 USA

[4] Argonne Natl Labs, Life Sci Collaborat Access Team, Argonne, IL 60439 USA

[5] BiOMaDe Technol Fdn, Groningen, Netherlands

来源：

SCIENCE | 2006年 / 311卷 / 5766期

关键词：

D O I：

10.1126/science.1121422

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Nisin is a posttranslationally modified antimicrobial peptide that is widely used as a food preservative. It contains five cyclic thioethers of varying sizes that are installed by a single enzyme, NisC. Reported here are the in vitro reconstitution of the cyclization process and the x-ray crystal structure of the NisC enzyme. The structure reveals similarities in fold and substrate activation with mammalian farnesyl transferases, suggesting that human homologs of NisC posttranslationally modify a cysteine of a protein substrate.

引用

页码：1464 / 1467

页数：4

共 33 条

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