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

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 and Jeffrey Green ()
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Bassam K. Kudhair: University of Sheffield
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
Nick E. Brun: University of East Anglia
Michael P. Williamson: University of Sheffield
Jeffrey Green: University of Sheffield

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: 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.

Date: 2017
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DOI: 10.1038/s41467-017-02418-y

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