1HAN
CRYSTAL STRUCTURE OF THE BIPHENYL-CLEAVING EXTRADIOL DIOXYGENASE FROM A PCB-DEGRADING PSEUDOMONAD
Summary for 1HAN
| Entry DOI | 10.2210/pdb1han/pdb |
| Descriptor | 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE, FE (III) ION, TERTIARY-BUTYL ALCOHOL, ... (4 entities in total) |
| Functional Keywords | extradiol dioxygenase, oxidoreductase (oxygenase) |
| Biological source | Burkholderia xenovorans |
| Total number of polymer chains | 1 |
| Total formula weight | 32563.41 |
| Authors | Han, S.,Bolin, J.T. (deposition date: 1995-08-30, release date: 1995-11-14, Last modification date: 2024-02-07) |
| Primary citation | Han, S.,Eltis, L.D.,Timmis, K.N.,Muchmore, S.W.,Bolin, J.T. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science, 270:976-980, 1995 Cited by PubMed Abstract: 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. PubMed: 7481800PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
