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@ARTICLE{Kosinas:601037,
      author       = {Kosinas, Christos and Zerva, Anastasia and Topakas,
                      Evangelos and Dimarogona, Maria},
      title        = {{S}tructure–function studies of a novel laccase-like
                      multicopper oxidase from {T}hermothelomyces thermophila
                      provide insights into its biological role},
      journal      = {Acta crystallographica / Section D},
      volume       = {79},
      number       = {7},
      issn         = {0907-4449},
      address      = {Bognor Regis},
      publisher    = {Wiley},
      reportid     = {PUBDB-2024-00074},
      pages        = {641 - 654},
      year         = {2023},
      abstract     = {Multicopper oxidases are promiscuous biocatalysts with
                      great potential for the production of industrial compounds.
                      This study is focused on the elucidation of the
                      structure–function determinants of a novel laccase-like
                      multicopper oxidase from the thermophilic fungus
                      Thermothelomyces thermophila (TtLMCO1), 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 TtLMCO1, determined using an AlphaFold2 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 TtLMCO1 to oxidize ortho-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.},
      cin          = {EMBL-User},
      ddc          = {530},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / iNEXT-Discovery -
                      Infrastructure for transnational access and discovery in
                      structural biology (871037)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(EU-Grant)871037},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37326583},
      UT           = {WOS:001020462200009},
      doi          = {10.1107/S2059798323004175},
      url          = {https://bib-pubdb1.desy.de/record/601037},
}