This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1han
From Proteopedia
|
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
Page seeded by OCA on Tue Nov 20 16:29:15 2007
