5OAY
M. tuberculosis [4Fe-4S] protein WhiB1 is a four-helix bundle that forms a NO-sensitive complex with sigmaA and regulates the major virulence factor ESX-1
Summary for 5OAY
| Entry DOI | 10.2210/pdb5oay/pdb |
| NMR Information | BMRB: 34153 |
| Descriptor | Transcriptional regulator WhiB1, IRON/SULFUR CLUSTER (2 entities in total) |
| Functional Keywords | nitric oxide, sigmaa, iron-sulfur, tuberculosis, wbl protein, signaling protein |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Cellular location | Cytoplasm : P9WF43 |
| Total number of polymer chains | 1 |
| Total formula weight | 10735.32 |
| Authors | Williamson, M.P.,Green, J.,Hounslow, A.M. (deposition date: 2017-06-25, release date: 2018-01-03, Last modification date: 2024-05-15) |
| Primary citation | Kudhair, B.K.,Hounslow, A.M.,Rolfe, M.D.,Crack, J.C.,Hunt, D.M.,Buxton, R.S.,Smith, L.J.,Le Brun, N.E.,Williamson, M.P.,Green, J. Structure of a Wbl protein and implications for NO sensing by M. tuberculosis. Nat Commun, 8:2280-2280, 2017 Cited by PubMed 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 (σ) 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. PubMed: 29273788DOI: 10.1038/s41467-017-02418-y PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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