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. Le Brun; Michael P. Williamson; Jeffrey Green

doi:10.1038/s41467-017-02418-y

Nature Communications (Dec 2017)

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. Le Brun,
Michael P. Williamson,
Jeffrey Green

Affiliations

Bassam K. Kudhair: Molecular Biology and Biotechnology, University of Sheffield
Andrea M. Hounslow: Molecular Biology and Biotechnology, University of Sheffield
Matthew D. Rolfe: Molecular Biology and Biotechnology, University of Sheffield
Jason C. Crack: Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia
Debbie M. Hunt: Division of Mycobacterial Research, MRC National Institute for Medical Research
Roger S. Buxton: Division of Mycobacterial Research, MRC National Institute for Medical Research
Laura J. Smith: Molecular Biology and Biotechnology, University of Sheffield
Nick E. Le Brun: Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia
Michael P. Williamson: Molecular Biology and Biotechnology, University of Sheffield
Jeffrey Green: Molecular Biology and Biotechnology, University of Sheffield

DOI: https://doi.org/10.1038/s41467-017-02418-y
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 12

Abstract

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Mycobacterium tuberculosis WhiB1 is a DNA-binding protein with a NO sensitive [4Fe-4S] cluster. Here the authors present the NMR structure of WhiB1 and suggest how loss of the iron-sulfur cluster through nitrosylation affects WhiB1 DNA binding and leads to transcriptional reprogramming.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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