2H6B

Crystal structure of oxidized CprK in complex with o-chlorophenolacetic acid

Summary for 2H6B

• Entry DOI: 10.2210/pdb2h6b/pdb
• Descriptor: ChloroPhenol Reduction gene K, SULFATE ION, (3-CHLORO-4-HYDROXYPHENYL)ACETIC ACID, ... (4 entities in total)
• Functional Keywords: halorespiration, dna binding, chlorinated ligand, chlorophenol, cprk, helix-turn-helix, dna binding protein
• Biological source: Desulfitobacterium hafniense
• Total number of polymer chains: 2
• Total formula weight: 57356.68

Authors

Joyce, M.G.,Levy, C.,Leys, D. (deposition date: 2006-05-31, release date: 2006-07-04, Last modification date: 2024-11-13)

Primary citation

Joyce, M.G.,Levy, C.,Pop, S.M.,Biehl, B.D.,Doukov, T.I.,Ryter, J.M.,Mazon, H.,Smidt, H.,van den Heuvel, R.H.,Ragsdale, S.W.,van der Oost, J.,Leys, D.
CprK Crystal Structures Reveal Mechanism for Transcriptional Control of Halorespiration.
J.Biol.Chem., 281:28318-28325, 2006

PubMed Abstract: Halorespiration is a bacterial respiratory process in which haloorganic compounds act as terminal electron acceptors. This process is controlled at transcriptional level by CprK, a member of the ubiquitous CRP-FNR family. Here we present the crystal structures of oxidized CprK in presence of the ligand ortho-chlorophenolacetic acid and of reduced CprK in absence of this ligand. These structures reveal that highly specific binding of chlorinated, rather than the corresponding non-chlorinated, phenolic compounds in the NH(2)-terminal beta-barrels causes reorientation of these domains with respect to the central alpha-helix at the dimer interface. Unexpectedly, the COOH-terminal DNA-binding domains dimerize in the non-DNA binding state. We postulate the ligand-induced conformational change allows formation of interdomain contacts that disrupt the DNA domain dimer interface and leads to repositioning of the helix-turn-helix motifs. These structures provide a structural framework for further studies on transcriptional control by CRP-FNR homologs in general and of halorespiration regulation by CprK in particular.

PubMed: 16803881
DOI: 10.1074/jbc.M602654200

Experimental method

X-RAY DIFFRACTION (2.2 Å)