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http://purl.uniprot.org/citations/17642515http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17642515http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17642515http://www.w3.org/2000/01/rdf-schema#comment"The biotin carboxylase (BC) domain of pyruvate carboxylase (PC) from Bacillus thermodenitrificans (BC-bPC) was crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6, b = 116.0, c = 115.7 A. Two BC protomers are contained in the asymmetric unit. Diffraction data were collected at 100 K and the crystal structure was solved by the molecular-replacement method and refined against reflections in the 20.0-2.4 A resolution range, giving an R factor of 0.235 and a free R factor of 0.292. The overall structure of BC-bPC is similar to those of the BC subunits of Aquifex aeolicus PC (BC-aPC) and Escherichia coli ACC (BC-eACC). The crystal structure revealed that BC-bPC forms a unique dimeric quaternary structure, which might be caused as a result of the division of the BC domain from the rest of the protein. The position of domain B in BC-bPC differs from those in other enzymes of similar structure (BC-aPC and BC-eACC)."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.org/dc/terms/identifier"doi:10.1107/S0907444907029423"xsd:string
http://purl.uniprot.org/citations/17642515http://purl.org/dc/terms/identifier"doi:10.1107/s0907444907029423"xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Islam M.N."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Islam M.N."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Kondo H."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Kondo H."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Kondo S."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Kondo S."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Nakajima Y."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Nakajima Y."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Sugio S."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Sugio S."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Sueda S."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/author"Sueda S."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/name"Acta Crystallogr D Biol Crystallogr"xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/pages"885-890"xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/pages"885-890"xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/title"Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans."xsd:string
http://purl.uniprot.org/citations/17642515http://purl.uniprot.org/core/title"Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans."xsd:string