3E5X

OCPA complexed CprK

Summary for 3E5X

• Entry DOI: 10.2210/pdb3e5x/pdb
• Related: 3E5Q 3E5U 3E6B 3E6C 3E6D
• Descriptor: Cyclic nucleotide-binding protein, (3-CHLORO-4-HYDROXYPHENYL)ACETIC ACID (3 entities in total)
• Functional Keywords: cprk, halorespiration, transcriptional regulator, transcription regulation
• Biological source: Desulfitobacterium hafniense
• Total number of polymer chains: 4
• Total formula weight: 114515.70

Authors

Levy, C. (deposition date: 2008-08-14, release date: 2008-12-09, Last modification date: 2024-02-21)

Primary citation

Levy, C.,Pike, K.,Heyes, D.J.,Joyce, M.G.,Gabor, K.,Smidt, H.,van der Oost, J.,Leys, D.
Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator
Mol.Microbiol., 70:151-167, 2008

PubMed 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.

PubMed: 18717788
DOI: 10.1111/j.1365-2958.2008.06399.x

Experimental method

X-RAY DIFFRACTION (1.999 Å)