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http://purl.uniprot.org/citations/12581638http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12581638http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12581638http://www.w3.org/2000/01/rdf-schema#comment"ModE is a bacterial transcriptional regulator that orchestrates many aspects of molybdenum metabolism by binding to specific DNA sequences in a molybdate-dependent fashion. We present the crystal structure of Escherichia coli ModE in complex with molybdate, which was determined at 2.75A from a merohedrally twinned crystal (twin fraction approximately 0.30) with space group P4(3). We now have structures of ModE in both its "switched on" (ligand-bound) and "switched off" (apo) states. Comparison with the apo structure shows that ligand binding leads to extensive conformational changes not only in the molybdate-binding domain, but also in the DNA-binding domain. The most obvious difference is the loss of the pronounced asymmetry between the two chains of the ModE dimer, which had been a characteristic property of the apo structure. Another major change concerns the relative orientation of the two DNA-interacting winged helix-turn-helix motifs. Manual docking of an idealized DNA structure suggests that this conformational change should improve DNA binding of the activated molybdate-bound ModE."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.org/dc/terms/identifier"doi:10.1016/s0022-2836(02)01358-x"xsd:string
http://purl.uniprot.org/citations/12581638http://purl.org/dc/terms/identifier"doi:10.1016/s0022-2836(02)01358-x"xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/author"Hunter W.N."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/author"Hunter W.N."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/author"Schuttelkopf A.W."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/author"Schuttelkopf A.W."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/author"Boxer D.H."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/author"Boxer D.H."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/pages"761-767"xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/pages"761-767"xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/title"Crystal structure of activated ModE reveals conformational changes involving both oxyanion and DNA-binding domains."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/title"Crystal structure of activated ModE reveals conformational changes involving both oxyanion and DNA-binding domains."xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/volume"326"xsd:string
http://purl.uniprot.org/citations/12581638http://purl.uniprot.org/core/volume"326"xsd:string
http://purl.uniprot.org/citations/12581638http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12581638
http://purl.uniprot.org/citations/12581638http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12581638
http://purl.uniprot.org/citations/12581638http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12581638
http://purl.uniprot.org/citations/12581638http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12581638