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Article dans une revue
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.
https://hal.univ-grenoble-alpes.fr/hal-01991812
Contributeur : Frank Thomas <>
Soumis le : jeudi 24 janvier 2019 - 09:54:41
Dernière modification le : vendredi 6 novembre 2020 - 04:19:24
Contributeur : Frank Thomas <>
Soumis le : jeudi 24 janvier 2019 - 09:54:41
Dernière modification le : vendredi 6 novembre 2020 - 04:19:24
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