Structural highlights
Function
[BPHC_BURXL] Shows a preference for catechols with groups immediately adjacent to the hydroxyl substituents.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Polychlorinated biphenyls (PCBs) typify a class of stable aromatic pollutants that are targeted by bioremediation strategies. In the aerobic degradation of biphenyl by bacteria, the key step of ring cleavage is catalyzed by an Fe(II)-dependent extradiol dioxygenase. The crystal structure of 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB-degrading strain of Pseudomonas cepacia has been determined at 1.9 angstrom resolution. The monomer comprises amino- and carboxyl-terminal domains. Structural homology between and within the domains reveals evolutionary relationships within the extradiol dioxygenase family. The iron atom has five ligands in square pyramidal geometry: one glutamate and two histidine side chains, and two water molecules.
Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad.,Han S, Eltis LD, Timmis KN, Muchmore SW, Bolin JT Science. 1995 Nov 10;270(5238):976-80. PMID:7481800[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Han S, Eltis LD, Timmis KN, Muchmore SW, Bolin JT. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science. 1995 Nov 10;270(5238):976-80. PMID:7481800
