Volbeda, Anne, Pellicer Martinez, Ma Teresa, Crack, Jason C., Amara, Patricia, Gigarel, Océane, Munnoch, John T., Hutchings, Matthew I., Darnault, Claudine, Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061 and Fontecilla-Camps, Juan C. (2019) 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, 141 (6). 2367–2375. ISSN 0002-7863
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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.
Item Type: | Article |
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Faculty \ School: | Faculty of Science > School of Chemistry (former - to 2024) Faculty of Science Faculty of Science > School of Biological Sciences |
UEA Research Groups: | Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes |
Depositing User: | LivePure Connector |
Date Deposited: | 22 Jan 2019 10:30 |
Last Modified: | 08 Dec 2024 01:29 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/69645 |
DOI: | 10.1021/jacs.8b10823 |
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