4C0X

The crystal strucuture of PpAzoR in complex with anthraquinone-2- sulfonate

4C0X の概要

• エントリーDOI: 10.2210/pdb4c0x/pdb
• 分子名称: FMN-DEPENDENT NADH-AZOREDUCTASE 1, FLAVIN MONONUCLEOTIDE, 9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, azoreductase, nad(p)h quinone oxidoreductase
• 由来する生物種: PSEUDOMONAS PUTIDA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22731.42

構造登録者

Goncalves, A.M.D.,de Sanctis, D.,Bento, I. (登録日: 2013-08-08, 公開日: 2013-10-30, 最終更新日: 2023-12-20)

主引用文献

Goncalves, A.M.D.,Mendes, S.,De Sanctis, D.,Martins, L.O.,Bento, I.
The Crystal Structure of Pseudomonas Putida Azor: The Active Site Revisited.
FEBS J., 280:6643-, 2013

PubMed Abstract: The enzymatic degradation of azo dyes begins with the reduction of the azo bond. In this article, we report the crystal structures of the native azoreductase from Pseudomonas putida MET94 (PpAzoR) (1.60 Å), of PpAzoR in complex with anthraquinone-2-sulfonate (1.50 Å), and of PpAzoR in complex with Reactive Black 5 dye (1.90 Å). These structures reveal the residues and subtle changes that accompany substrate binding and release. Such changes highlight the fine control of access to the catalytic site that is required by the ping-pong mechanism, and in turn the specificity offered by the enzyme towards different substrates. The topology surrounding the active site shows novel features of substrate recognition and binding that help to explain and differentiate the substrate specificity observed among different bacterial azoreductases.

PubMed: 24127652
DOI: 10.1111/FEBS.12568

実験手法

X-RAY DIFFRACTION (1.499 Å)