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

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 be-tween +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 conformation-al change, centered on Trp9, which results in a significant shift in the DNA-binding helix-turn-helix region.
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Submitted on : Thursday, January 24, 2019 - 9:54:41 AM
Last modification on : Tuesday, June 11, 2019 - 8:26:45 AM

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Anne Volbeda, Ma Teresa Pellicer Martinez, Jason Crack, Patricia Amara, Océane Gigarel, et al.. Crystal Structure of the Transcription Regulator RsrR Reveals a [2Fe-2S] Cluster Coordinated by Cys, Glu and His Residues.. Journal of the American Chemical Society, American Chemical Society, 2019, 141 (6), pp.2367-2375. ⟨10.1021/jacs.8b10823⟩. ⟨hal-01991812⟩

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