| http://purl.uniprot.org/citations/14747735 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14747735 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14747735 | http://www.w3.org/2000/01/rdf-schema#comment | "4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a central enzyme in the metabolism of phenolic compounds in anaerobic bacteria. The enzyme catalyzes the reductive removal of the phenolic hydroxyl group from 4-hydroxybenzoyl-CoA, yielding benzoyl-CoA and water. 4-HBCR belongs to the xanthine oxidase (XO) family of molybdenum enzymes which occur as heterodimers, (alphabetagamma)(2). 4-HBCR contains two molybdopterins, four [2Fe-2S] and two [4Fe-4S] clusters and two FADs. A low-potential Allochromatium vinosum-type ferredoxin containing two [4Fe-4S] clusters serves as an in vivo electron donor for 4-HBCR. In this work, the oxygen-sensitive proteins 4-HBCR and the ferredoxin (TaFd) from Thauera aromatica were crystallized under anaerobic conditions. 4-HBCR crystallized with PEG 4000 and MPD as precipitant diffracted to about 1.6 A resolution and the crystals were highly suitable for X-ray structure analysis. Crystals of TaFd were obtained with (NH(4))(3)PO(4) as precipitant and revealed a solvent content of 77%, which is remarkably high for a small soluble protein. The structure of TaFd was solved at 2.9 A resolution by the molecular-replacement method using the highly related structure of the ferredoxin (CvFd) from A. vinosum as a model. Structural changes between the two ferredoxins around the [4Fe-4S] cluster can be correlated with their different redox potentials."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.org/dc/terms/identifier | "doi:10.1107/S0907444903028506"xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444903028506"xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/author | "Boll M."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/author | "Boll M."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/author | "Ermler U."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/author | "Ermler U."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/author | "Warkentin E."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/author | "Warkentin E."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/author | "Unciuleac M."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/author | "Unciuleac M."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/name | "Acta Crystallogr. D"xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/name | "Acta Crystallogr D Biol Crystallogr"xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/pages | "388-391"xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/pages | "388-391"xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/title | "Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/title | "Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin."xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/volume | "60"xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://purl.uniprot.org/core/volume | "60"xsd:string |
| http://purl.uniprot.org/citations/14747735 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14747735 |
| http://purl.uniprot.org/citations/14747735 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14747735 |