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DOI | 10.2210/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: 26440996DOI: 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
検証レポート(詳細版)
をダウンロード






