5I68

Alcohol oxidase from Pichia pastoris

5I68 の概要

• エントリーDOI: 10.2210/pdb5i68/pdb
• EMDBエントリー: 8072
• 分子名称: Alcohol oxidase 1, MAGNESIUM ION, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: alcohol oxidase peroxisome, oxidoreductase
• 由来する生物種: Komagataella pastoris (Yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 74802.05

構造登録者

Vonck, J.,Mills, D.J.,Parcej, D.N. (登録日: 2016-02-16, 公開日: 2016-08-03, 最終更新日: 2024-05-15)

主引用文献

Vonck, J.,Parcej, D.N.,Mills, D.J.
Structure of Alcohol Oxidase from Pichia pastoris by Cryo-Electron Microscopy.
Plos One, 11:e0159476-e0159476, 2016

PubMed Abstract: The first step in methanol metabolism in methylotrophic yeasts, the oxidation of methanol and higher alcohols with molecular oxygen to formaldehyde and hydrogen peroxide, is catalysed by alcohol oxidase (AOX), a 600-kDa homo-octamer containing eight FAD cofactors. When these yeasts are grown with methanol as the carbon source, AOX forms large crystalline arrays in peroxisomes. We determined the structure of AOX by cryo-electron microscopy at a resolution of 3.4 Å. All residues of the 662-amino acid polypeptide as well as the FAD are well resolved. AOX shows high structural homology to other members of the GMC family of oxidoreductases, which share a conserved FAD binding domain, but have different substrate specificities. The preference of AOX for small alcohols is explained by the presence of conserved bulky aromatic residues near the active site. Compared to the other GMC enzymes, AOX contains a large number of amino acid inserts, the longest being 75 residues. These segments are found at the periphery of the monomer and make extensive inter-subunit contacts which are responsible for the very stable octamer. A short surface helix forms contacts between two octamers, explaining the tendency of AOX to form crystals in the peroxisomes.

PubMed: 27458710
DOI: 10.1371/journal.pone.0159476

実験手法

ELECTRON MICROSCOPY (3.37 Å)