http://purl.uniprot.org/citations/17642515 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17642515 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17642515 | http://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/17642515 | http://purl.org/dc/terms/identifier | "doi:10.1107/S0907444907029423"xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444907029423"xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Islam M.N."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Islam M.N."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Kondo H."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Kondo H."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Kondo S."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Kondo S."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Nakajima Y."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Nakajima Y."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Sugio S."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Sugio S."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Sueda S."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/author | "Sueda S."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/name | "Acta Crystallogr. D"xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/name | "Acta Crystallogr D Biol Crystallogr"xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/pages | "885-890"xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/pages | "885-890"xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/title | "Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans."xsd:string |
http://purl.uniprot.org/citations/17642515 | http://purl.uniprot.org/core/title | "Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans."xsd:string |