Walton, Paul Howard orcid.org/0000-0002-1152-1480, Labourel, Aurore, Frandsen, Kristian E H et al. (17 more authors) (2020) A fungal family of lytic polysaccharide monooxygenase-like copper proteins. NATURE CHEMICAL BIOLOGY. https://doi.org/10.1038/s41589-019-0438-8. pp. 1-11. ISSN 1552-4450
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2020 Springer Nature Limited. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Funding Information: | Funder Grant number BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL) BB/R007705/1 |
Depositing User: | Pure (York) |
Date Deposited: | 11 Feb 2020 11:40 |
Last Modified: | 12 Jan 2025 00:07 |
Published Version: | https://doi.org/10.1038/s41589-019-0438-8 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1038/s41589-019-0438-8 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:156810 |
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Filename: X325_SI_after_last_review.pdf
Description: X325 SI after last review