Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
D GoldstoneP Metcalf

Abstract

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.

References

Jan 14, 2003·Annual Review of Biochemistry·Hiroshi KadokuraJon Beckwith
Jun 5, 2003·Acta Crystallographica. Section D, Biological Crystallography·Rebecca PageScott A Lesley

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