| http://purl.uniprot.org/citations/16453738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16453738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16453738 | http://www.w3.org/2000/01/rdf-schema#comment | "The three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Rhodospirillum rubrum has been determined at 2.9 A resolution by X-ray crystallographic methods. The MIR-electron density map was substantially improved by two-fold non-crystallographic symmetry averaging. The polypeptide chains in the dimer were traced using a graphics display system with the help of the BONES option in FRODO. The dimer has approximate dimensions of 50 x 72 x 105 A. The enzyme subunit is a typical two-domain protein. The smaller, N-terminal domain consists of 137 amino acid residues and forms a central, mixed five-stranded beta-sheet with alpha-helices on both sides of the sheet. The larger C-terminal domain consists of 329 amino acid residues. This domain has an eight-stranded parallel alpha/beta barrel structure as found in triosephosphate isomerase and a number of other functionally non-related proteins. The active site in Rubisco determined by difference Fourier techniques and fitting of active site residues to the electron density map, is located at the carboxy-end of the beta-strands in the alpha/beta barrel of the C-terminal domain. There are few domain-domain interactions within the subunit. The interactions at the interface between the two subunits of the dimer are tight and extensive. There are tight contacts between the two C-terminal domains, which build up the core of the molecule. There are also interactions between the N-terminal domain of one subunit and the C-terminal domain of the second subunit, close to the active site."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.org/dc/terms/identifier | "doi:10.1002/j.1460-2075.1986.tb04662.x"xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.org/dc/terms/identifier | "doi:10.1002/j.1460-2075.1986.tb04662.x"xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/author | "Schneider G."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/author | "Schneider G."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/author | "Braenden C.-I."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/author | "Braenden C.-I."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/author | "Lindqvist Y."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/author | "Lindqvist Y."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/author | "Lorimer G."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/author | "Lorimer G."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/pages | "3409-3415"xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/pages | "3409-3415"xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/title | "Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/title | "Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution."xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/16453738 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16453738 |
| http://purl.uniprot.org/citations/16453738 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16453738 |