1EIQ

2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE

1EIQ の概要

• エントリーDOI: 10.2210/pdb1eiq/pdb
• 関連するPDBエントリー: 1DHY 1EIL 1EIM 1EIR
• 分子名称: 2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE, FE (III) ION (3 entities in total)
• 機能のキーワード: four repetitions of beta-alpha-beta-beta-beta motifs, oxidoreductase
• 由来する生物種: Pseudomonas sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32207.39

構造登録者

Senda, T. (登録日: 2000-02-28, 公開日: 2001-02-28, 最終更新日: 2024-02-07)

主引用文献

Uragami, Y.,Senda, T.,Sugimoto, K.,Sato, N.,Nagarajan, V.,Masai, E.,Fukuda, M.,Mitsu, Y.
Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase.
J.Inorg.Biochem., 83:269-279, 2001

PubMed 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.

PubMed: 11293547
DOI: 10.1016/S0162-0134(00)00172-0

実験手法

X-RAY DIFFRACTION (2 Å)