2GBW
Crystal Structure of Biphenyl 2,3-Dioxygenase from Sphingomonas yanoikuyae B1
Summary for 2GBW
| Entry DOI | 10.2210/pdb2gbw/pdb |
| Related | 2GBX |
| Descriptor | Biphenyl 2,3-Dioxygenase Alpha Subunit, Biphenyl 2,3-Dioxygenase Beta Subunit, FE (III) ION, ... (6 entities in total) |
| Functional Keywords | rieske oxygenase, oxidoreductase, non heme iron, dioxygenase |
| Biological source | Sphingobium yanoikuyae More |
| Total number of polymer chains | 6 |
| Total formula weight | 216260.69 |
| Authors | Ferraro, D.J.,Brown, E.N.,Yu, C.,Parales, R.E.,Gibson, D.T.,Ramaswamy, S. (deposition date: 2006-03-12, release date: 2007-03-20, Last modification date: 2023-08-30) |
| Primary citation | Ferraro, D.J.,Brown, E.N.,Yu, C.L.,Parales, R.E.,Gibson, D.T.,Ramaswamy, S. Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1. Bmc Struct.Biol., 7:10-10, 2007 Cited by PubMed Abstract: The initial step involved in oxidative hydroxylation of monoaromatic and polyaromatic compounds by the microorganism Sphingobium yanoikuyae strain B1 (B1), previously known as Sphingomonas yanoikuyae strain B1 and Beijerinckia sp. strain B1, is performed by a set of multiple terminal Rieske non-heme iron oxygenases. These enzymes share a single electron donor system consisting of a reductase and a ferredoxin (BPDO-FB1). One of the terminal Rieske oxygenases, biphenyl 2,3-dioxygenase (BPDO-OB1), is responsible for B1's ability to dihydroxylate large aromatic compounds, such as chrysene and benzo[a]pyrene. PubMed: 17349044DOI: 10.1186/1472-6807-7-10 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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