Journal:Acta Cryst D:S2059798323004175
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | This study presents the crystal structure of a novel laccase-like multicopper oxidase from a thermophilic fungus (''Thermothelomyces thermophila''), named ''Tt''LMCO1. Multicopper oxidases are biocatalysts with various biotechnological applications, such as wastewater treatment, synthesis of novel bioactive compounds, lignin degradation as well as biosensors development. This study is focused on TtLMCO1, which is capable of oxidizing both ascorbic acid and phenolic compounds and is thus functionally categorized between ascorbate oxidases and fungal laccases. The crystal structure of ''Tt''LMCO1, determined using an AlphaFold 2.0 model in 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 with substrates that are oxidized by | + | This study presents the crystal structure of a novel laccase-like multicopper oxidase from a thermophilic fungus (''Thermothelomyces thermophila''), named ''Tt''LMCO1. Multicopper oxidases are biocatalysts with various biotechnological applications, such as wastewater treatment, synthesis of novel bioactive compounds, lignin degradation as well as biosensors development. This study is focused on TtLMCO1, which is capable of oxidizing both ascorbic acid and phenolic compounds and is thus functionally categorized between ascorbate oxidases and fungal laccases. The crystal structure of ''Tt''LMCO1, determined using an AlphaFold 2.0 model in 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 with substrates that are oxidized by ''Tt''LMCO1 provide evidence that substrate specificity of these metallo-proteins is not exclusively related to their redox potential but also on the architecture of the binding site and the side chain flexibility of specific amino acids. Also, our analysis points to a potential biological role of these biocatalysts, involving the production of pigments and other bioactive compounds in their natural hosts. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 11:48, 17 May 2023
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