1eil
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2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE
OverviewOverview
BphC derived from Pseudomonas sp. strain KKS102, an extradiol type, catecholic dioxygenase, is a non-heam iron-containing enzyme, playing an, important role in the degradation of biphenyl/PCB (Poly Chlorinated, Biphenyls) in the microbe. Although we had earlier solved the crystal, structure of KKS102 BphC, it was the inactive form with Fe(III) in the, active site. In order to determine the active form structure, BphC was, re-activated by anaerobic incubation with Fe(II) and ascorbate, and, crystallized anaerobically. The crystal structures of activated BphC and, its substrate complex (E x S complex) were determined at 2.0 A resolution, under cryogenic condition. In addition, crystal structures of unactivated, BphC in substrate free and complex forms were also re-determined., Comparison of activated and unactivated E x S complexes reveals that the, orientation of the bound substrate in the active site is significantly, different between the two. The structural comparison of the substrate free, and complex forms of activated BphC show certain small conformational, shifts around the active site upon substrate binding. As a result of the, conformational shifts, His194, which has been suggested as the catalytic, base, takes part in a weak hydrogen bond with hydroxyl group of the, substrate.
About this StructureAbout this Structure
1EIL is a Single protein structure of sequence from Pseudomonas sp. with SO4 and FE as ligands. The following page contains interesting information on the relation of 1EIL with [Topoisomerases]. Active as Biphenyl-2,3-diol 1,2-dioxygenase, with EC number 1.13.11.39 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase., Uragami Y, Senda T, Sugimoto K, Sato N, Nagarajan V, Masai E, Fukuda M, Mitsu Y, J Inorg Biochem. 2001 Feb;83(4):269-79. PMID:11293547
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