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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/2329585 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2329585 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2329585 | http://www.w3.org/2000/01/rdf-schema#comment | "The crystal structure of flavocytochrome b2 has been solved at 3.0 A resolution by the method of multiple isomorphous replacement with anomalous scattering. Area detector data from native and two heavy-atom derivative crystals were used. The phases were refined by the B.C. Wang phase-filtering procedure utilizing the 67% (v/v) solvent content of the crystals. A molecular model was built first on a minimap and then on computer graphics from a combination of maps both averaged and not averaged about the molecular symmetry axis. The structure was extended to 2.4 A resolution using film data recorded at a synchrotron and refined by the Hendrickson-Konnert procedure. The molecule, a tetramer of Mr 230,000, is located on a crystallographic 2-fold axis and possesses local 4-fold symmetry. Each subunit is composed of two domains, one binding a heme and the other an FMN prosthetic group. In subunit 1, both the cystochrome and the flavin-binding domain are visible in the electron density map. In subunit 2 the cytochrome domain is disordered. However, in the latter, a molecule of pyruvate, the product of the enzymatic reaction, is bound at the active site. The cytochrome domain consists of residues 1 to 99 and is folded in a fashion similar to the homologous soluble fragment of cytochrome b5. The flavin binding domain contains a parallel beta 8 alpha 8 barrel structure and is composed of residues 100 to 486. The remaining 25 residues form a tail that wraps around the molecular 4-fold axis and is in contact with each remaining subunit. The FMN moiety, which is located at the C-terminal end of the central beta-barrel, is mostly sequestered from solvent; it forms hydrogen bond interactions with main- and side-chain atoms from six of the eight beta-strands. The interaction of Lys349 with atoms N-1 and O-2 of the flavin ring is probably responsible for stabilization of the anionic form of the flavin semiquinone and hydroquinone and enhancing the reactivity of atom N-5 toward sulfite. The binding of pyruvate at the active site in subunit 2 is stabilized by interaction of its carboxylate group with the side-chain atoms of Arg376 and Tyr143. Residues His373 and Tyr254 interact with the keto-oxygen atom and are involved in catalysis. In contrast, four water molecules occupy the substrate-binding site in subunit 1 and Tyr143 forms a hydrogen bond to the ordered heme propionate group. Otherwise the two flavin-binding domains are identical within experimental error.(ABSTRACT TRUNCATED AT 400 WORDS)"xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.org/dc/terms/identifier | "doi:10.1016/0022-2836(90)90240-m"xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.org/dc/terms/identifier | "doi:10.1016/0022-2836(90)90240-m"xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/author | "Mathews F.S."xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/author | "Mathews F.S."xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/author | "Xia Z.-X."xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/author | "Xia Z.-X."xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/pages | "837-863"xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/pages | "837-863"xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/title | "Molecular structure of flavocytochrome b2 at 2.4-A resolution."xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/title | "Molecular structure of flavocytochrome b2 at 2.4-A resolution."xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/volume | "212"xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://purl.uniprot.org/core/volume | "212"xsd:string |
| http://purl.uniprot.org/citations/2329585 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2329585 |
| http://purl.uniprot.org/citations/2329585 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2329585 |
| http://purl.uniprot.org/citations/2329585 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2329585 |
| http://purl.uniprot.org/citations/2329585 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2329585 |
| http://purl.uniprot.org/uniprot/P00175 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2329585 |
| http://purl.uniprot.org/uniprot/P00175#attribution-BADDAF90C4FFA4C6AE86D6398A29D19A | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/2329585 |