Crystal structures of the NO sensor NsrR reveal how its iron-sulfur cluster modulates DNA binding

Anne Volbeda, Erin L. Dodd, Claudine Darnault, Jason C. Crack, Oriane Renoux, Matthew I. Hutchings, Nick E. Le Brun () and Juan C. Fontecilla-Camps ()
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Anne Volbeda: Metalloproteins Unit, Institut de Biologie Structurale, CEA, CNRS, Université Grenoble-Alpes
Erin L. Dodd: Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich Research Park
Claudine Darnault: Metalloproteins Unit, Institut de Biologie Structurale, CEA, CNRS, Université Grenoble-Alpes
Jason C. Crack: Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich Research Park
Oriane Renoux: Metalloproteins Unit, Institut de Biologie Structurale, CEA, CNRS, Université Grenoble-Alpes
Matthew I. Hutchings: School of Biological Sciences, University of East Anglia, Norwich Research Park
Nick E. Le Brun: Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich Research Park
Juan C. Fontecilla-Camps: Metalloproteins Unit, Institut de Biologie Structurale, CEA, CNRS, Université Grenoble-Alpes

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract NsrR from Streptomyces coelicolor (Sc) regulates the expression of three genes through the progressive degradation of its [4Fe–4S] cluster on nitric oxide (NO) exposure. We report the 1.95 Å resolution crystal structure of dimeric holo-ScNsrR and show that the cluster is coordinated by the three invariant Cys residues from one monomer and, unexpectedly, Asp8 from the other. A cavity map suggests that NO displaces Asp8 as a cluster ligand and, while D8A and D8C variants remain NO sensitive, DNA binding is affected. A structural comparison of holo-ScNsrR with an apo-IscR-DNA complex shows that the [4Fe–4S] cluster stabilizes a turn between ScNsrR Cys93 and Cys99 properly oriented to interact with the DNA backbone. In addition, an apo ScNsrR structure suggests that Asn97 from this turn, along with Arg12, which forms a salt-bridge with Asp8, are instrumental in modulating the position of the DNA recognition helix region relative to its major groove.

Date: 2017
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DOI: 10.1038/ncomms15052

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