Journal:Acta Cryst D:S2059798323004175
From Proteopedia
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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 | + | 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 ''Tt''LMCO1, which is capable of oxidizing both ascorbic acid and phenolic compounds and is thus functionally categorized between ascorbate oxidases and fungal laccases. <scene name='96/965740/Overall/1'>The crystal structure of ''Tt''LMCO1</scene>, 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. The refined crystal structure of TtLMCO1 contains 576 residues arranged in three cupredoxin-like domains. Domain A includes residues 11 to 134, domain B includes residues 135-372 and domain C includes residues 373-602. A unique disulfide bond is formed between Cys28 and Cys236, stabilizing the relative orientation between domains A and B. |
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| + | 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 13:16, 17 May 2023
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