| Literature DB >> 25760714 |
Jincheng Li1, Xudong Wang2, Weimin Gong2, Chunyan Niu2, Min Zhang1.
Abstract
Adaptations to hypoxia play an important role in Mycobacterium tuberculosis pathogenesis. Rv0324, which contains an HTH DNA-binding domain and a rhodanese domain, is one of the key transcription regulators in response to hypoxia. M. tuberculosis Rv1674c is a homologue of Rv0324. To understand the interdomain interaction and regulation of the HTH domain and the rhodanese domain, recombinant Rv1674c protein was purified and crystallized by the vapour-diffusion method. The crystals diffracted to 2.25 Å resolution. Preliminary diffraction analysis suggests that the crystals belonged to space group P3121 or P3221, with unit-cell parameters a = b = 67.8, c = 174.5 Å, α = β = 90, γ = 120°. The Matthews coefficient was calculated to be 2.44 Å(3) Da(-1), assuming that the crystallographic asymmetric unit contains two protein molecules.Entities:
Keywords: HTH DNA-binding domain; Rv1674c; rhodanese domain
Mesh:
Substances:
Year: 2015 PMID: 25760714 PMCID: PMC4356315 DOI: 10.1107/S2053230X15001028
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056