Literature DB >> 26249679

Crystallographic studies of the extracytoplasmic function σ factor σ(J) from Mycobacterium tuberculosis.

Kapil Goutam1, Arvind Kumar Gupta1, Balasubramanian Gopal1.   

Abstract

Mycobacterium tuberculosis has multiple σ factors which enable the bacterium to reprogram its transcriptional machinery under diverse environmental conditions. σ(J), an extracytoplasmic function σ factor, is upregulated in late stationary phase cultures and during human macrophage infection. σ(J) governs the cellular response to hydrogen peroxide-mediated oxidative stress. σ(J) differs from other canonical σ factors owing to the presence of a SnoaL_2 domain at the C-terminus. σ(J) crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 133.85, c = 75.08 Å. Diffraction data were collected to 2.16 Å resolution on the BM14 beamline at the European Synchrotron Radiation Facility (ESRF).

Entities:  

Keywords:  SnoaL_2 domain; potential drug target; sigma factor; σ factor

Mesh:

Substances:

Year:  2015        PMID: 26249679      PMCID: PMC4528921          DOI: 10.1107/S2053230X15009577

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


  23 in total

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Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2011-03-18

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  1 in total

1.  The fused SnoaL_2 domain in the Mycobacterium tuberculosis sigma factor σJ modulates promoter recognition.

Authors:  Kapil Goutam; Arvind K Gupta; Balasubramanian Gopal
Journal:  Nucleic Acids Res       Date:  2017-09-19       Impact factor: 16.971

  1 in total

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