File:Structure-of-Alcohol-Oxidase-from-Pichia-pastoris-by-Cryo-Electron-Microscopy-pone.0159476.s006.ogv

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English: The AOX octamer with domain colors shown. Colors are as in Fig 5a: FAD-binding domain (red); FAD covering lid (pink); extended FAD-binding domain (yellow); flavin attachment loop (green) and intermediate region (light green); substrate-binding domain (cyan). Helix H12, which forms crystal contacts, is shown in orange. The longest AOX-specific insert 481–548 is shown in dark blue, other AOX-specific sequences are colored purple. The tetramer interface is exclusively made by AOX-specific elements (dark blue and purple).
Date
Source S5 Movie from Vonck J, Parcej D, Mills D (2016). "Structure of Alcohol Oxidase from Pichia pastoris by Cryo-Electron Microscopy". PLOS ONE. DOI:10.1371/journal.pone.0159476. PMID 27458710. PMC: 4961394.
Author Vonck J, Parcej D, Mills D
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current02:20, 18 August 20167.2 s, 822 × 670 (24.19 MB)Open Access Media Importer Bot (talk | contribs)Automatically uploaded media file from Open Access source. Please report problems or suggestions here.

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VP9 480P 1.33 Mbps Completed 20:49, 20 October 2018 44 s
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