Structure of the Staphylococcus aureus AgrA LytTR domain bound to DNA reveals a beta fold with an unusual mode of binding

被引：112

作者：

Sidote, David J. ^{[1
,2
]}

Barbieri, Christopher M. ^{[1
,2
]}

Wu, Ti ^{[1
,2
]}

Stock, Ann M. ^{[1
,2
]}

机构：

[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Ctr Adv Biotechnol & Med, Howard Hughes Med Inst, Piscataway, NJ 08854 USA

[2] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Howard Hughes Med Inst, Piscataway, NJ 08854 USA

来源：

STRUCTURE | 2008年 / 16卷 / 05期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/j.str.2008.02.011

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 LytTR domain is a DNA-binding motif found within the AlgR/AgrA/LytR family of transcription factors that regulate virulence factor and toxin gene expression in pathogenic bacteria. This previously uncharacterized domain lacks sequence similarity with proteins of known structure. The crystal structure of the DNA-binding domain of Staphylococcus aureus AgrA complexed with a DNA pentadecamer duplex has been determined at 1.6 angstrom resolution. The structure establishes a 10-stranded beta fold for the LytTR domain and reveals its mode of interaction with DNA. Residues within loop regions of AgrA contact two successive major grooves and the intervening minor groove on one face of the oligonucleotide duplex, inducing a substantial bend in the DNA. Loss of DNA binding upon substitution of key interacting residues in AgrA supports the observed binding mode. This mode of protein-DNA interaction provides a potential target for future antimicrobial drug design.

引用

页码：727 / 735

页数：9

共 39 条

[1] THE ACCESSORY GENE REGULATOR (AGR) CONTROLS STAPHYLOCOCCUS-AUREUS VIRULENCE IN A MURINE ARTHRITIS MODEL [J].