TY - JOUR
T1 - Cloning, expression, crystallization and preliminary X-ray analysis of a putative multiple antibiotic resistance repressor protein (MarR) from Xanthomonas campestris
AU - Tu, Zhi Le
AU - Li, Juo Ning
AU - Chin, Ko Hsin
AU - Chou, Chia Cheng
AU - Lee, Cheng Chung
AU - Shr, Hui Lin
AU - Lyu, Ping Chiang
AU - Gao, Fei Philip
AU - Wang, Andrew H.J.
AU - Chou, Shan Ho
PY - 2005/7
Y1 - 2005/7
N2 - 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 P212121, 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.
AB - 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 P212121, 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.
UR - http://www.scopus.com/inward/record.url?scp=33744460489&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33744460489&partnerID=8YFLogxK
U2 - 10.1107/S1744309105019548
DO - 10.1107/S1744309105019548
M3 - Article
C2 - 16511135
AN - SCOPUS:33744460489
SN - 1744-3091
VL - 61
SP - 706
EP - 708
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 7
ER -