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Publication Abstract from PubMed

Certain bacteria are able to conserve energy via the reductive dehalogenation of halo-organic compounds in a respiration-type metabolism. The transcriptional regulator CprK from Desulfitobacterium spp. induces expression of halorespiratory genes upon binding of o-chlorophenol ligands and is reversibly inactivated by oxygen through disulphide bond formation. We report crystal structures of D. hafniense CprK in the ligand-free (both oxidation states), ligand-bound (reduced) and DNA-bound states, making it the first member of the widespread CRP-FNR superfamily for which a complete structural description of both redox-dependent and allosteric molecular rearrangements is available. In conjunction with kinetic and thermodynamic ligand binding studies, we provide a model for the allosteric mechanisms underpinning transcriptional control. Amino acids that play a key role in this mechanism are not conserved in functionally distinct CRP-FNR members. This suggests that, despite significant structural homology, distinct allosteric mechanisms are used, enabling this protein family to control a very wide range of processes.

Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator.,Levy C, Pike K, Heyes DJ, Joyce MG, Gabor K, Smidt H, van der Oost J, Leys D Mol Microbiol. 2008 Oct;70(1):151-67. Epub 2008 Aug 20. PMID:18717788^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.