Open AccessCrystallization and preliminary diffraction studies of the C‐terminal domain of the DipZ homologue from Mycobacterium tuberculosis
Author(s) -
Goldstone David,
Baker Edward N.,
Metcalf Peter
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105001909
Subject(s) - mycobacterium tuberculosis , escherichia coli , disulfide bond , thioredoxin , transmembrane protein , crystallography , crystallization , transmembrane domain , chemistry , domain (mathematical analysis) , stereochemistry , biochemistry , tuberculosis , membrane , gene , receptor , organic chemistry , medicine , mathematical analysis , mathematics , pathology
Protein disulfide‐bond formation is poorly understood in the pathogenic bacterium Mycobacterium tuberculosis. Rv2874 is the M. tuberculosis homologue of the disulfide‐bond electron transporter DsbD from Escherichia coli . Both proteins share a core central transmembrane domain and a C‐terminal thioredoxin domain. To investigate the possible role of Rv2874 in disulfide‐bond formation in M. tuberculosis , the C‐terminal domain of Rv2874 has been cloned, expressed, purified and crystallized. The crystals belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 109.7, b = 118.3, c = 122.9 Å, and diffract to at least 3.0 Å.