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http://purl.uniprot.org/citations/16260765http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16260765http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16260765http://www.w3.org/2000/01/rdf-schema#comment"YdhR is a 101-residue conserved protein from Escherichia coli. Sequence searches reveal that the protein has >50% identity to proteins found in a variety of other bacterial genomes. Using size exclusion chromatography and fluorescence spectroscopy, we determined that ydhR exists in a dimeric state with a dissociation constant of approximately 40 nM. The three-dimensional structure of dimeric ydhR was determined using NMR spectroscopy. A total of 3400 unambiguous NOEs, both manually and automatically assigned, were used for the structure calculation that was refined using an explicit hydration shell. A family of 20 structures was obtained with a backbone RMSD of 0.48 A for elements of secondary structure. The structure reveals a dimeric alpha,beta fold characteristic of the alpha+beta barrel superfamily of proteins. Bioinformatic approaches were used to show that ydhR likely belongs to a recently identified group of mono-oxygenase proteins that includes ActVA-Orf6 and YgiN and are involved in the oxygenation of polyaromatic ring compounds."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.org/dc/terms/identifier"doi:10.1110/ps.051809305"xsd:string
http://purl.uniprot.org/citations/16260765http://purl.org/dc/terms/identifier"doi:10.1110/ps.051809305"xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/author"Semesi A."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/author"Semesi A."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/author"Yee A."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/author"Yee A."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/author"Shaw G.S."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/author"Shaw G.S."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/author"Revington M."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/author"Revington M."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/pages"3115-3120"xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/pages"3115-3120"xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/title"Solution structure of the Escherichia coli protein ydhR: a putative mono-oxygenase."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/title"Solution structure of the Escherichia coli protein ydhR: a putative mono-oxygenase."xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/16260765http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/16260765http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16260765
http://purl.uniprot.org/citations/16260765http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16260765