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|Title:||Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator|
Heyes, D. J.
Joyce, M. Gordon
van der Oost, J.
|Citation:||Molecular Microbiology (2008) 70(1), 151–167|
|Abstract:||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.|
|Rights:||© 2008 The Authors|
|Appears in Collections:||Published Articles, Dept. of Biochemistry|
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