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This study is focused on the elucidation of the structure\u2013function determinants of a novel laccase-like multicopper oxidase from the thermophilic fungus\n                    <jats:italic>Thermothelomyces thermophila<\/jats:italic>\n                    (\n                    <jats:italic>Tt<\/jats:italic>\n                    LMCO1), which is capable of oxidizing both ascorbic acid and phenolic compounds and thus is functionally categorized between the ascorbate oxidases and fungal ascomycete laccases (asco-laccases). The crystal structure of\n                    <jats:italic>Tt<\/jats:italic>\n                    LMCO1, determined using an\n                    <jats:italic>AlphaFold<\/jats:italic>\n                    2 model due to a lack of experimentally determined structures of close homologues, revealed a three-domain laccase with two copper sites, lacking the C-terminal plug observed in other asco-laccases. Analysis of solvent tunnels highlighted the amino acids that are crucial for proton transfer into the trinuclear copper site. Docking simulations showed that the ability of\n                    <jats:italic>Tt<\/jats:italic>\n                    LMCO1 to oxidize\n                    <jats:italic>ortho<\/jats:italic>\n                    -substituted phenols stems from the movement of two polar amino acids at the hydrophilic side of the substrate-binding region, providing structural evidence for the promiscuity of this enzyme.\n                  <\/jats:p>","DOI":"10.1107\/s2059798323004175","type":"journal-article","created":{"date-parts":[[2023,5,30]],"date-time":"2023-05-30T09:19:32Z","timestamp":1685438372000},"page":"641-654","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":4,"title":["Structure\u2013function studies of a novel laccase-like multicopper oxidase from\n                    <i>Thermothelomyces thermophila<\/i>\n                    provide insights into its biological role"],"prefix":"10.1107","volume":"79","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5479-7858","authenticated-orcid":true,"given":"Christos","family":"Kosinas","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/017wvtq80","id-type":"ROR","asserted-by":"publisher"}],"department":["Laboratory of Structural Biology and Biotechnology, Department of Chemical Engineering"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0361-7690","authenticated-orcid":true,"given":"Anastasia","family":"Zerva","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03cx6bg69","id-type":"ROR","asserted-by":"publisher"}],"department":["Industrial Biotechnology and Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0078-5904","authenticated-orcid":true,"given":"Evangelos","family":"Topakas","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03cx6bg69","id-type":"ROR","asserted-by":"publisher"}],"department":["Industrial Biotechnology and Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5663-1421","authenticated-orcid":true,"given":"Maria","family":"Dimarogona","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/017wvtq80","id-type":"ROR","asserted-by":"publisher"}],"department":["Laboratory of Structural Biology and Biotechnology, Department of Chemical Engineering"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2023,6,16]]},"reference":[{"key":"jc5058_bb55","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1107\/S2059798323003595","volume":"79","author":"Agirre","year":"2023","journal-title":"Acta Cryst. 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