1HAN
CRYSTAL STRUCTURE OF THE BIPHENYL-CLEAVING EXTRADIOL DIOXYGENASE FROM A PCB-DEGRADING PSEUDOMONAD
1HAN の概要
| エントリーDOI | 10.2210/pdb1han/pdb |
| 分子名称 | 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE, FE (III) ION, TERTIARY-BUTYL ALCOHOL, ... (4 entities in total) |
| 機能のキーワード | extradiol dioxygenase, oxidoreductase (oxygenase) |
| 由来する生物種 | Burkholderia xenovorans |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 32563.41 |
| 構造登録者 | |
| 主引用文献 | 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: 7481800主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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