7ZJB

Structural and functional characterization of the bacterial lytic polysaccharide Monooxygenase ScLPMO10D

7ZJB の概要

• エントリーDOI: 10.2210/pdb7zjb/pdb
• 分子名称: Putative secreted cellulose-binding protein, COPPER (II) ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: lpmo, aa10, oxidoreductase
• 由来する生物種: Streptomyces coelicolor A3(2)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20214.41

構造登録者

Votvik, A.K.,Rohr, A.K.,Stepnov, A.A.,Bissaro, B.,Sorlie, M.,Eijsink, V.G.H.,Forsberg, Z. (登録日: 2022-04-10, 公開日: 2023-04-19, 最終更新日: 2024-11-06)

主引用文献

Votvik, A.K.,Rohr, A.K.,Bissaro, B.,Stepnov, A.A.,Sorlie, M.,Eijsink, V.G.H.,Forsberg, Z.
Structural and functional characterization of the catalytic domain of a cell-wall anchored bacterial lytic polysaccharide monooxygenase from Streptomyces coelicolor.
Sci Rep, 13:5345-5345, 2023

PubMed Abstract: Bacterial lytic polysaccharide monooxygenases (LPMOs) are known to oxidize the most abundant and recalcitrant polymers in Nature, namely cellulose and chitin. The genome of the model actinomycete Streptomyces coelicolor A3(2) encodes seven putative LPMOs, of which, upon phylogenetic analysis, four group with typical chitin-oxidizing LPMOs, two with typical cellulose-active LPMOs, and one which stands out by being part of a subclade of non-characterized enzymes. The latter enzyme, called ScLPMO10D, and most of the enzymes found in this subclade are unique, not only because of variation in the catalytic domain, but also as their C-terminus contains a cell wall sorting signal (CWSS), which flags the LPMO for covalent anchoring to the cell wall. Here, we have produced a truncated version of ScLPMO10D without the CWSS and determined its crystal structure, EPR spectrum, and various functional properties. While showing several structural and functional features typical for bacterial cellulose active LPMOs, ScLPMO10D is only active on chitin. Comparison with two known chitin-oxidizing LPMOs of different taxa revealed interesting functional differences related to copper reactivity. This study contributes to our understanding of the biological roles of LPMOs and provides a foundation for structural and functional comparison of phylogenetically distant LPMOs with similar substrate specificities.

PubMed: 37005446
DOI: 10.1038/s41598-023-32263-7

実験手法

X-RAY DIFFRACTION (1.37 Å)