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

dc.cclicenceCC-BYen
dc.contributor.authorKudhair, B.K.en
dc.contributor.authorHounslow, A.M.en
dc.contributor.authorRolfe, Matthew D.en
dc.contributor.authorCrack, Jason C.en
dc.contributor.authorHunt, Debbie M.en
dc.contributor.authorBuxton, Roger S.en
dc.contributor.authorSmith, Laura J.en
dc.contributor.authorLe Brun, Nick E.en
dc.contributor.authorWilliamson, M.P.en
dc.contributor.authorGreen , J.en
dc.date.acceptance2017-11-29en
dc.date.accessioned2018-04-16T10:53:52Z
dc.date.available2018-04-16T10:53:52Z
dc.date.issued2017-12-22
dc.description.abstractMycobacterium 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.en
dc.exception.reasonThe output was published as gold open accessen
dc.funderBBSRCen
dc.identifier.citationKudhair, B.K. et al., 2017. Structure of a Wbl protein and implications for NO sensing by M. tuberculosis. Nature Communications, 8(1).en
dc.identifier.doihttps://doi.org/10.1038/s41467-017-02418-y
dc.identifier.urihttp://hdl.handle.net/2086/16023
dc.language.isoen_USen
dc.peerreviewedYesen
dc.projectidN/Aen
dc.publisherNature Publishing Groupen
dc.researchgroupInfectious Disease Research Groupen
dc.researchinstituteLeicester Institute for Pharmaceutical Innovation - From Molecules to Practice (LIPI)en
dc.subjectMetalloproteins, Wbl, transcription factor, NMRen
dc.titleStructure of a Wbl protein and implications for NO sensing by M. tuberculosisen
dc.typeArticleen

Files

Original bundle
Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
s41467-017-02418-y.pdf
Size:
3.12 MB
Format:
Adobe Portable Document Format
Description:
Main article
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
4.2 KB
Format:
Item-specific license agreed upon to submission
Description: