TY  - JOUR
A1  - Vonck, Janet
A1  - Parcej, David
A1  - Mills, Deryck J.
T1  - Structure of alcohol oxidase from pichia pastoris by cryo-electron microscopy
T2  - PLoS one
N2  - 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.
Y1  - 2016
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/41442
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-414422
UR  - https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4961394/
SN  - 1932-6203
N1  - Copyright: © 2016 Vonck et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
VL  - 11
IS  - (7): e0159476
SP  - 1
EP  - 20
PB  - PLoS
CY  - Lawrence, Kan.
ER  -