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http://purl.uniprot.org/citations/12429099http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12429099http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12429099http://www.w3.org/2000/01/rdf-schema#comment"The Obg nucleotide binding protein family has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to man. Members of the family contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain. Structural analysis of Bacillus subtilis Obg revealed respective domain architectures and how they are coupled through the putative switch elements of the C-terminal GTPase domain in apo and nucleotide-bound configurations. Biochemical analysis of bacterial and human Obg proteins combined with the structural observation of the ppGpp nucleotide within the Obg active sight suggest a potential role for ppGpp modulation of Obg function in B. subtilis."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(02)00882-1"xsd:string
http://purl.uniprot.org/citations/12429099http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(02)00882-1"xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/author"Lima C.D."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/author"Lima C.D."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/author"Shen V."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/author"Shen V."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/author"Buglino J."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/author"Buglino J."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/author"Hakimian P."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/author"Hakimian P."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/pages"1581-1592"xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/pages"1581-1592"xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/title"Structural and biochemical analysis of the Obg GTP binding protein."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/title"Structural and biochemical analysis of the Obg GTP binding protein."xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/12429099http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/12429099http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12429099
http://purl.uniprot.org/citations/12429099http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12429099