7zn6 | pdb_00007zn6

Crystal structure of laccase-like multicopper oxidase (LMCO) from Thermothelomyces thermophilus

spinqualitylabelsall models 7zn6, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7zn6 is a 1 chain structure with sequence from Thermothelomyces thermophilus ATCC 42464. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CU, EDO, GOL, NAG, OXY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LMCO1_MYCTT Yellow laccase-like multicopper oxidase that is able to oxidize a variety of phenolic compounds including standard laccase substrates such as 2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,6-dimethoxyphenol (2,6-DMP) (PubMed:30529567). Can be used for the bioconversion of 2',3,4-trihy-droxychalcone to 3',4'-dihydroxy-aurone, a bioactive aurone recently shown to possess inhibitory activity against several isoforms of the histone deacetylase complex (HDAC) (PubMed:30529567). Publication Abstract from PubMed 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. Structure-function studies of a novel laccase-like multicopper oxidase from Thermothelomyces thermophila provide insights into its biological role.,Kosinas C, Zerva A, Topakas E, Dimarogona M Acta Crystallogr D Struct Biol. 2023 Jul 1;79(Pt 7):641-654. doi: , 10.1107/S2059798323004175. Epub 2023 Jun 16. PMID:37326583 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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