1han
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(New page: 200px<br /><applet load="1han" size="450" color="white" frame="true" align="right" spinBox="true" caption="1han, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 14:22, 20 November 2007
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CRYSTAL STRUCTURE OF THE BIPHENYL-CLEAVING EXTRADIOL DIOXYGENASE FROM A PCB-DEGRADING PSEUDOMONAD
Overview
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.
About this Structure
1HAN is a Single protein structure of sequence from Burkholderia cepacia with FE and TBU as ligands. Active as Biphenyl-2,3-diol 1,2-dioxygenase, with EC number 1.13.11.39 Full crystallographic information is available from OCA.
Reference
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
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