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

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.

Bibliographic Details
Main Authors:	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
Format:	Article
Language:	English
Published:	Nature Publishing Group 2017-12-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-017-02418-y

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spelling	doaj-a3161fc00cf1472d8753db514aa76e062021-05-11T07:28:13ZengNature Publishing GroupNature Communications2041-17232017-12-018111210.1038/s41467-017-02418-yStructure of a Wbl protein and implications for NO sensing by M. tuberculosisBassam K. Kudhair0Andrea M. Hounslow1Matthew D. Rolfe2Jason C. Crack3Debbie M. Hunt4Roger S. Buxton5Laura J. Smith6Nick E. Le Brun7Michael P. Williamson8Jeffrey Green9Molecular Biology and Biotechnology, University of SheffieldMolecular Biology and Biotechnology, University of SheffieldMolecular Biology and Biotechnology, University of SheffieldCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East AngliaDivision of Mycobacterial Research, MRC National Institute for Medical ResearchDivision of Mycobacterial Research, MRC National Institute for Medical ResearchMolecular Biology and Biotechnology, University of SheffieldCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East AngliaMolecular Biology and Biotechnology, University of SheffieldMolecular Biology and Biotechnology, University of SheffieldMycobacterium 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.https://doi.org/10.1038/s41467-017-02418-y
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	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
spellingShingle	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 Structure of a Wbl protein and implications for NO sensing by M. tuberculosis Nature Communications
author_facet	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
author_sort	Bassam K. Kudhair
title	Structure of a Wbl protein and implications for NO sensing by M. tuberculosis
title_short	Structure of a Wbl protein and implications for NO sensing by M. tuberculosis
title_full	Structure of a Wbl protein and implications for NO sensing by M. tuberculosis
title_fullStr	Structure of a Wbl protein and implications for NO sensing by M. tuberculosis
title_full_unstemmed	Structure of a Wbl protein and implications for NO sensing by M. tuberculosis
title_sort	structure of a wbl protein and implications for no sensing by m. tuberculosis
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2017-12-01
description	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.
url	https://doi.org/10.1038/s41467-017-02418-y
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Structure of a Wbl protein and implications for NO sensing by M. tuberculosis

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