5UIZ

Structure of T.fusca AA10A

「4GBO」から置き換えられました

5UIZ の概要

• エントリーDOI: 10.2210/pdb5uiz/pdb
• 分子名称: AA10A, COPPER (II) ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: aa10a, polysaccharide monooxygenase, oxidoreductase, e7, lpmo, lyase
• 由来する生物種: Thermobifida fusca
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54573.13

構造登録者

Alahuhta, P.M.,Lunin, V.V. (登録日: 2017-01-16, 公開日: 2017-02-01, 最終更新日: 2024-10-23)

主引用文献

Kruer-Zerhusen, N.,Alahuhta, M.,Lunin, V.V.,Himmel, M.E.,Bomble, Y.J.,Wilson, D.B.
Structure of a Thermobifida fusca lytic polysaccharide monooxygenase and mutagenesis of key residues.
Biotechnol Biofuels, 10:243-243, 2017

PubMed Abstract: Auxiliary activity (AA) enzymes are produced by numerous bacterial and fungal species to assist in the degradation of biomass. These enzymes are abundant but have yet to be fully characterized. Here, we report the X-ray structure of AA10A (TfAA10A), investigate mutational characterization of key surface residues near its active site, and explore the importance of the various domains of AA10B (TfAA10B). The structure of TfAA10A is similar to other bacterial LPMOs (lytic polysaccharide monooxygenases), including signs of photo-reduction and a distorted active site, with mixed features showing both type I and II copper coordination. The point mutation experiments of TfAA10A show that Trp82 and Asn83 are needed for binding, but only Trp82 affects activity. The TfAA10B domain truncation mutants reveal that CBM2 is crucial for the binding of substrate, but that the X1 module does not affect binding or activity.

PubMed: 29213309
DOI: 10.1186/s13068-017-0925-7

実験手法

X-RAY DIFFRACTION (2 Å)