Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis

Bo Li; John Paul J. Yu; Joseph S. Brunzelle; Gert N. Moll; Wilfred A. Van Der Donk; Satish K. Nair

doi:10.1126/science.1121422

Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis

Bo Li, John Paul J. Yu, Joseph S. Brunzelle, Gert N. Moll, Wilfred A. Van Der Donk, Satish K. Nair

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English (US)
Pages (from-to)	1464-1467
Number of pages	4
Journal	Science
Volume	311
Issue number	5766
DOIs	https://doi.org/10.1126/science.1121422
State	Published - Mar 10 2006

ASJC Scopus subject areas

General

Online availability

10.1126/science.1121422

Library availability

Discover UIUC Full Text

Cite this

@article{f848cf8a8a6c4c108d23f7706987ac55,

title = "Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis",

abstract = "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.",

author = "Bo Li and Yu, {John Paul J.} and Brunzelle, {Joseph S.} and Moll, {Gert N.} and {Van Der Donk}, {Wilfred A.} and Nair, {Satish K.}",

year = "2006",

month = mar,

day = "10",

doi = "10.1126/science.1121422",

language = "English (US)",

volume = "311",

pages = "1464--1467",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "5766",

}

TY - JOUR

T1 - Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis

AU - Li, Bo

AU - Yu, John Paul J.

AU - Brunzelle, Joseph S.

AU - Moll, Gert N.

AU - Van Der Donk, Wilfred A.

AU - Nair, Satish K.

PY - 2006/3/10

Y1 - 2006/3/10

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=33644854595&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33644854595&partnerID=8YFLogxK

U2 - 10.1126/science.1121422

DO - 10.1126/science.1121422

M3 - Article

C2 - 16527981

AN - SCOPUS:33644854595

SN - 0036-8075

VL - 311

SP - 1464

EP - 1467

JO - Science

JF - Science

IS - 5766

ER -

Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis

Abstract

ASJC Scopus subject areas

Online availability

Library availability

Related links

Fingerprint

Cite this