Open AccessCloning, expression, crystallization and preliminary X‐ray analysis of a putative multiple antibiotic resistance repressor protein (MarR) from Xanthomonas campestris
Author(s) -
Tu ZhiLe,
Li JuoNing,
Chin KoHsin,
Chou ChiaCheng,
Lee ChengChung,
Shr HuiLin,
Lyu PingChiang,
Gao Fei Philip,
Wang Andrew H.J.,
Chou ShanHo
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105019548
Subject(s) - cloning (programming) , xanthomonas campestris , repressor , microbiology and biotechnology , biology , crystallization , xanthomonas , chemistry , gene , genetics , gene expression , organic chemistry , computer science , programming language
The multiple antibiotic resistance operon ( marRAB ) is a member of the multidrug‐resistance system. When induced, this operon enhances resistance of bacteria to a variety of medically important antibiotics, causing a serious global health problem. MarR is a marR ‐encoded protein that represses the transcription of the marRAB operon. Through binding with salicylate and certain antibiotics, however, MarR can derepress and activate the marRAB operon. In this report, the cloning, expression, crystallization and preliminary X‐ray analysis of XC1739, a putative MarR repressor protein present in the Xanthomonas campestris pv. campestris , a Gram‐negative bacterium causing major worldwide disease of cruciferous crops, are described. The XC1739 crystals diffracted to a resolution of at least 1.8 Å. They are orthorhombic and belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 39.5, b = 54.2 and c = 139.5 Å, respectively. They contain two molecules in the asymmetric unit from calculation of the self‐rotation function.