6HSD

Crystal structure of the oxidized form of the transcription regulator RsrR

Summary for 6HSD

• Entry DOI: 10.2210/pdb6hsd/pdb
• Descriptor: Rrf2 family transcriptional regulator, FE2/S2 (INORGANIC) CLUSTER, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (6 entities in total)
• Functional Keywords: redox sensor, iron sulfur cluster, transcription
• Biological source: Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)
• Total number of polymer chains: 4
• Total formula weight: 72193.11

Authors

Volbeda, A.,Fontecilla-Camps, J.C. (deposition date: 2018-09-30, release date: 2019-01-30, Last modification date: 2024-05-15)

Primary citation

Volbeda, A.,Martinez, M.T.P.,Crack, J.C.,Amara, P.,Gigarel, O.,Munnoch, J.T.,Hutchings, M.I.,Darnault, C.,Le Brun, N.E.,Fontecilla-Camps, J.C.
Crystal Structure of the Transcription Regulator RsrR Reveals a [2Fe-2S] Cluster Coordinated by Cys, Glu, and His Residues.
J. Am. Chem. Soc., 141:2367-2375, 2019

PubMed 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.

PubMed: 30657661
DOI: 10.1021/jacs.8b10823

Experimental method

X-RAY DIFFRACTION (1.6 Å)