PDBsum entry: 1eil

Oxidoreductase

PDB id: 1eil

Contents

Protein chain

289 a.a. *

Ligands

SO4

Metals

_FE

Waters ×193

* Residue conservation analysis

PDB id:

1eil

Name:

Oxidoreductase

Title:

2,3-dihydroxybiphenyl-1,2-dioxygenase

Structure:

2,3-dihydroxybiphenyl 1,2-dioxygenase. Chain: a. Synonym: biphenyl-2,3-diol 1,2-dioxygenase, 23 ohbp oxygena engineered: yes

Source:

Pseudomonas sp.. Organism_taxid: 307. Strain: kks102. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Octamer (from PDB file)

Resolution:

2.00Å R-factor: 0.206 R-free: 0.253

Authors:

T.Senda

Key ref:

Y.Uragami et al. (2001). Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase. J Inorg Biochem, 83, 269-279. PubMed id: 11293547 DOI: 10.1016/S0162-0134(00)00172-0

Date:

26-Feb-00 Release date: 26-Feb-01

Protein chain

P17297  (BPHC_PSES1) -  Biphenyl-2,3-diol 1,2-dioxygenase

Seq: 293 a.a.

Struc: 289 a.a.

Enzyme reactions

• Enzyme class: E.C.1.13.11.39 - Biphenyl-2,3-diol 1,2-dioxygenase.
• Reaction: Biphenyl-2,3-diol + O₂ = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
• Cofactor: Manganese or iron

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: oxidation-reduction process (4 terms)
• Biochemical function: catalytic activity (8 terms)

reference

DOI no: 10.1016/S0162-0134(00)00172-0

J Inorg Biochem 83:269-279 (2001)

PubMed id: 11293547

Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase.

Y.Uragami, T.Senda, K.Sugimoto, N.Sato, V.Nagarajan, E.Masai, M.Fukuda, Y.Mitsu.

ABSTRACT

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.