Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis.
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 P2(1)2(1)2(1), with unit-cell parameters a = 109.7, b = 118.3, c = 122.9 A, and diffract to at least 3.0 A.
Goldstone
David
D
School of Biological Science, University of Auckland, Auckland, New Zealand.
Baker
Edward N
EN
Metcalf
Peter
P
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D017931:DNA Primers; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000235:genetics; D010088:Oxidoreductases; D010957:Plasmids; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D017931:DNA Primers; C079503:DsbB protein, Bacteria; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D011994:Recombinant Proteins; D010088:Oxidoreductases; C094848:DsbD electron transport protein, E coli