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Structure of a Wbl protein and implications for NO sensing by M. tuberculosis

Author

Listed:
  • Bassam K. Kudhair

    (University of Sheffield
    University of Kufa)

  • Andrea M. Hounslow

    (University of Sheffield)

  • Matthew D. Rolfe

    (University of Sheffield)

  • Jason C. Crack

    (University of East Anglia)

  • Debbie M. Hunt

    (MRC National Institute for Medical Research)

  • Roger S. Buxton

    (MRC National Institute for Medical Research)

  • Laura J. Smith

    (University of Sheffield
    De Montfort University)

  • Nick E. Brun

    (University of East Anglia)

  • Michael P. Williamson

    (University of Sheffield)

  • Jeffrey Green

    (University of Sheffield)

Abstract

Mycobacterium tuberculosis causes pulmonary tuberculosis (TB) and claims ~1.8 million human lives per annum. Host nitric oxide (NO) is important in controlling TB infection. M. tuberculosis WhiB1 is a NO-responsive Wbl protein (actinobacterial iron–sulfur proteins first identified in the 1970s). Until now, the structure of a Wbl protein has not been available. Here a NMR structural model of WhiB1 reveals that Wbl proteins are four-helix bundles with a core of three α-helices held together by a [4Fe-4S] cluster. The iron–sulfur cluster is required for formation of a complex with the major sigma factor (σA) and reaction with NO disassembles this complex. The WhiB1 structure suggests that loss of the iron–sulfur cluster (by nitrosylation) permits positively charged residues in the C-terminal helix to engage in DNA binding, triggering a major reprogramming of gene expression that includes components of the virulence-critical ESX-1 secretion system.

Suggested Citation

  • Bassam K. Kudhair & Andrea M. Hounslow & Matthew D. Rolfe & Jason C. Crack & Debbie M. Hunt & Roger S. Buxton & Laura J. Smith & Nick E. Brun & Michael P. Williamson & Jeffrey Green, 2017. "Structure of a Wbl protein and implications for NO sensing by M. tuberculosis," Nature Communications, Nature, vol. 8(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-02418-y
    DOI: 10.1038/s41467-017-02418-y
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    Cited by:

    1. Nelson V. Simwela & Luana Johnston & Paulina Pavinski Bitar & Eleni Jaecklein & Craig Altier & Christopher M. Sassetti & David G. Russell, 2024. "Genome-wide screen of Mycobacterium tuberculosis-infected macrophages revealed GID/CTLH complex-mediated modulation of bacterial growth," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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