6IBJ

Copper binding protein from Laetisaria arvalis (LaX325)

6IBJ の概要

• エントリーDOI: 10.2210/pdb6ibj/pdb
• 関連するPDBエントリー: 6IBH 6IBI
• 分子名称: Auxiliary activity CAZyme, 2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: auxiliary activity cazyme, metal binding protein
• 由来する生物種: Laetisaria arvalis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17612.40

構造登録者

Frandsen, K.E.H.,Tandrup, T.,Labourel, A.,Haon, M.,Berrin, J.-G.,Lo Leggio, L. (登録日: 2018-11-30, 公開日: 2019-11-13, 最終更新日: 2024-10-16)

主引用文献

Labourel, A.,Frandsen, K.E.H.,Zhang, F.,Brouilly, N.,Grisel, S.,Haon, M.,Ciano, L.,Ropartz, D.,Fanuel, M.,Martin, F.,Navarro, D.,Rosso, M.N.,Tandrup, T.,Bissaro, B.,Johansen, K.S.,Zerva, A.,Walton, P.H.,Henrissat, B.,Leggio, L.L.,Berrin, J.G.
A fungal family of lytic polysaccharide monooxygenase-like copper proteins.
Nat.Chem.Biol., 16:345-350, 2020

PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that play a key role in the oxidative degradation of various biopolymers such as cellulose and chitin. While hunting for new LPMOs, we identified a new family of proteins, defined here as X325, in various fungal lineages. The three-dimensional structure of X325 revealed an overall LPMO fold and a His brace with an additional Asp ligand to Cu(II). Although LPMO-type activity of X325 members was initially expected, we demonstrated that X325 members do not perform oxidative cleavage of polysaccharides, establishing that X325s are not LPMOs. Investigations of the biological role of X325 in the ectomycorrhizal fungus Laccaria bicolor revealed exposure of the X325 protein at the interface between fungal hyphae and tree rootlet cells. Our results provide insights into a family of copper-containing proteins, which is widespread in the fungal kingdom and is evolutionarily related to LPMOs, but has diverged to biological functions other than polysaccharide degradation.

PubMed: 31932718
DOI: 10.1038/s41589-019-0438-8

実験手法

X-RAY DIFFRACTION (2.1 Å)