1han | pdb_00001han

CRYSTAL STRUCTURE OF THE BIPHENYL-CLEAVING EXTRADIOL DIOXYGENASE FROM A PCB-DEGRADING PSEUDOMONAD

spinqualitylabelsall models 1han, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1han is a 1 chain structure with sequence from Burkholderia xenovorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, TBU Gene: BPHC (Burkholderia xenovorans) Activity: Biphenyl-2,3-diol 1,2-dioxygenase, with EC number 1.13.11.39 Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dioxygenase

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