Literature DB >> 25760714

Crystallization and preliminary X-ray analysis of Rv1674c from Mycobacterium tuberculosis.

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


  11 in total

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