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J Am Chem Soc. 2019 Feb 13;141(6):2367-2375. doi: 10.1021/jacs.8b10823. Epub 2019 Feb 1.

Crystal Structure of the Transcription Regulator RsrR Reveals a [2Fe-2S] Cluster Coordinated by Cys, Glu, and His Residues.

Author information

1
Université Grenoble Alpes, CEA, CNRS , IBS , Metalloproteins Unit, F-38044 Grenoble , France.
2
Centre for Molecular and Structural Biochemistry, School of Chemistry , University of East Anglia , Norwich Research Park, Norwich NR4 7TJ , United Kingdom.
3
School of Biological Sciences , University of East Anglia , Norwich Research Park, Norwich NR4 7TJ , United Kingdom.

Abstract

The recently discovered Rrf2 family transcriptional regulator RsrR coordinates a [2Fe-2S] cluster. Remarkably, binding of the protein to RsrR-regulated promoter DNA sequences is switched on and off through the facile cycling of the [2Fe-2S] cluster between +2 and +1 states. Here, we report high resolution crystal structures of the RsrR dimer, revealing that the [2Fe-2S] cluster is asymmetrically coordinated across the RsrR monomer-monomer interface by two Cys residues from one subunit and His and Glu residues from the other. To our knowledge, this is the first example of a protein bound [Fe-S] cluster with three different amino acid side chains as ligands, and of Glu acting as ligand to a [2Fe-2S] cluster. Analyses of RsrR structures revealed a conformational change, centered on Trp9, which results in a significant shift in the DNA-binding helix-turn-helix region.

PMID:
30657661
DOI:
10.1021/jacs.8b10823

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