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3E5U

OCPA complexed CprK (C200S)

Summary for 3E5U
Entry DOI10.2210/pdb3e5u/pdb
Related3E5Q 3E5X 3E6B 3E6C 3E6D
DescriptorCyclic nucleotide-binding protein, (3-CHLORO-4-HYDROXYPHENYL)ACETIC ACID, PHOSPHATE ION, ... (5 entities in total)
Functional Keywordscprk, halorespiration, transcriptional regulator, transcription regulation
Biological sourceDesulfitobacterium hafniense
Total number of polymer chains4
Total formula weight114759.33
Authors
Levy, C. (deposition date: 2008-08-14, release date: 2008-09-30, Last modification date: 2024-02-21)
Primary citationLevy, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.83 Å)
Structure validation

237735

数据于2025-06-18公开中

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