| http://purl.uniprot.org/citations/15911615 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15911615 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15911615 | http://www.w3.org/2000/01/rdf-schema#comment | "Pyridoxal 5'-phosphate (PLP, vitamin B6), a cofactor in many enzymatic reactions, has two distinct biosynthetic routes, which do not coexist in any organism. Two proteins, known as PdxS and PdxT, together form a PLP synthase in plants, fungi, archaea, and some eubacteria. PLP synthase is a heteromeric glutamine amidotransferase in which PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. In the 2.2-A crystal structure, PdxS is a cylindrical dodecamer of subunits having the classic (beta/alpha)8 barrel fold. PdxS subunits form two hexameric rings with the active sites positioned on the inside. The hexamer and dodecamer forms coexist in solution. A novel phosphate-binding site is suggested by bound sulfate. The sulfate and another bound molecule, methyl pentanediol, were used to model the substrate ribulose 5-phosphate, and to propose catalytic roles for residues in the active site. The distribution of conserved surfaces in the PdxS dodecamer was used to predict a docking site for the glutaminase partner, PdxT."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m503642200"xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m503642200"xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Zhu J."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Zhu J."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Smith J.L."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Smith J.L."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Belitsky B.R."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Belitsky B.R."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Harms E."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Harms E."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Burgner J.W."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/author | "Burgner J.W."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/pages | "27914-27923"xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/pages | "27914-27923"xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/title | "A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/title | "A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase."xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/volume | "280"xsd:string |
| http://purl.uniprot.org/citations/15911615 | http://purl.uniprot.org/core/volume | "280"xsd:string |