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4CVC

Crystal structure of quinone-dependent alcohol dehydrogenase from Pseudogluconobacter saccharoketogenenes with zinc in the active site

4CVC の概要
エントリーDOI10.2210/pdb4cvc/pdb
関連するPDBエントリー4CVB
分子名称ALCOHOL DEHYDROGENASE, DI(HYDROXYETHYL)ETHER, PYRROLOQUINOLINE QUINONE, ... (7 entities in total)
機能のキーワードoxidoreductase, carbohydrate oxidation, quinoprotein
由来する生物種PSEUDOGLUCONOBACTER SACCHAROKETOGENES
タンパク質・核酸の鎖数1
化学式量合計62367.53
構造登録者
Rozeboom, H.J.,Yu, S.,Mikkelsen, R.,Nikolaev, I.,Mulder, H.,Dijkstra, B.W. (登録日: 2014-03-25, 公開日: 2015-03-25, 最終更新日: 2024-11-06)
主引用文献Rozeboom, H.J.,Yu, S.,Mikkelsen, R.,Nikolaev, I.,Mulder, H.J.,Dijkstra, B.W.
Crystal Structure of Quinone-Dependent Alcohol Dehydrogenase from Pseudogluconobacter Saccharoketogenes. A Versatile Dehydrogenase Oxidizing Alcohols and Carbohydrates.
Protein Sci., 24:2044-, 2015
Cited by
PubMed Abstract: The quinone-dependent alcohol dehydrogenase (PQQ-ADH, E.C. 1.1.5.2) from the Gram-negative bacterium Pseudogluconobacter saccharoketogenes IFO 14464 oxidizes primary alcohols (e.g. ethanol, butanol), secondary alcohols (monosaccharides), as well as aldehydes, polysaccharides, and cyclodextrins. The recombinant protein, expressed in Pichia pastoris, was crystallized, and three-dimensional (3D) structures of the native form, with PQQ and a Ca(2+) ion, and of the enzyme in complex with a Zn(2+) ion and a bound substrate mimic were determined at 1.72 Å and 1.84 Å resolution, respectively. PQQ-ADH displays an eight-bladed β-propeller fold, characteristic of Type I quinone-dependent methanol dehydrogenases. However, three of the four ligands of the Ca(2+) ion differ from those of related dehydrogenases and they come from different parts of the polypeptide chain. These differences result in a more open, easily accessible active site, which explains why PQQ-ADH can oxidize a broad range of substrates. The bound substrate mimic suggests Asp333 as the catalytic base. Remarkably, no vicinal disulfide bridge is present near the PQQ, which in other PQQ-dependent alcohol dehydrogenases has been proposed to be necessary for electron transfer. Instead an associated cytochrome c can approach the PQQ for direct electron transfer.
PubMed: 26440996
DOI: 10.1002/PRO.2818
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.83 Å)
構造検証レポート
Validation report summary of 4cvc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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