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http://purl.uniprot.org/citations/16803881http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16803881http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16803881http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.org/dc/terms/identifier"doi:10.1074/jbc.M602654200"xsd:string
http://purl.uniprot.org/citations/16803881http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m602654200"xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Leys D."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Leys D."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Ragsdale S.W."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Ragsdale S.W."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"van der Oost J."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"van der Oost J."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"van den Heuvel R.H."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"van den Heuvel R.H."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Smidt H."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Smidt H."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Doukov T.I."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Doukov T.I."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Levy C."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Levy C."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Joyce M.G."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Joyce M.G."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Mazon H."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Mazon H."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Pop S.M."xsd:string
http://purl.uniprot.org/citations/16803881http://purl.uniprot.org/core/author"Pop S.M."xsd:string