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2GBW

Crystal Structure of Biphenyl 2,3-Dioxygenase from Sphingomonas yanoikuyae B1

Summary for 2GBW
Entry DOI10.2210/pdb2gbw/pdb
Related2GBX
DescriptorBiphenyl 2,3-Dioxygenase Alpha Subunit, Biphenyl 2,3-Dioxygenase Beta Subunit, FE (III) ION, ... (6 entities in total)
Functional Keywordsrieske oxygenase, oxidoreductase, non heme iron, dioxygenase
Biological sourceSphingobium yanoikuyae
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Total number of polymer chains6
Total formula weight216260.69
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 citationFerraro, 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: 17349044
DOI: 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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