Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis

Multicopper oxidases (MCOs) represent a diverse family of enzymes that catalyze the oxidation of either an organic or a metal substrate with concomitant reduction of dioxygen to water. These enzymes contain variable numbers of cupredoxin domains, two, three or six per subunit, and rely on four coppe...

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Bibliographic Details
Published in:	Acta crystallographica. Section D, Biological crystallography. Vol. 77; no. 10; pp. 1336 - 1345
Main Authors:	Paavola, Joseph L., Battistin, Umberto, Ogata, Craig M., Georgiadis, Millie M.
Format:	Journal Article
Language:	English
Published:	5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-10-2021 Wiley Subscription Services, Inc IUCr
Subjects:	Bacteria - enzymology BASIC BIOLOGICAL SCIENCES Catalytic Domain Closed balls Copper Copper - metabolism Crystal structure Crystallography, X-Ray Decoloring Detoxification dodecamers Domains Dyes Electron transfer Enzymes Industrial wastes Laccase - metabolism laccases Marinithermus hydrothermalis Metal ions Models, Molecular multi-copper oxidases Multicopper oxidase multicopper oxidases Oxidation Oxidoreductases - chemistry Oxidoreductases - metabolism Protein Conformation Protein Multimerization Reduction (metal working) Research Papers Substrates thermophiles Trimers Marinithermus hydrothermalis crystal structure laccases dodecamers thermophiles multicopper oxidases
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Summary:	Multicopper oxidases (MCOs) represent a diverse family of enzymes that catalyze the oxidation of either an organic or a metal substrate with concomitant reduction of dioxygen to water. These enzymes contain variable numbers of cupredoxin domains, two, three or six per subunit, and rely on four copper ions, a single type I copper and three additional copper ions organized in a trinuclear cluster (TNC), with one type II and two type III copper ions, to catalyze the reaction. Here, two crystal structures and the enzymatic characterization of Marinithermus hydrothermalis MCO, a two‐domain enzyme, are reported. This enzyme decolorizes Congo Red dye at 70°C in the presence of high halide concentrations and may therefore be useful in the detoxification of industrial waste that contains dyes. In two distinct crystal structures, MhMCO forms the trimers seen in other two‐domain MCOs, but differs from these enzymes in that four trimers interact to create a dodecamer. This dodecamer of MhMCO forms a closed ball‐like structure and has implications for the sequestration of bound divalent metal ions as well as substrate accessibility. In each subunit of the dodecameric structures, a Trp residue, Trp351, located between the type I and TNC sites exists in two distinct conformations, consistent with a potential role in facilitating electron transfer in the enzyme. A two‐domain multicopper oxidase (MCO) from Marinithermus hydrothermalis functions as a laccase and was crystallized in two distinct lattices as a dodecameric ball‐like structure. Crystal structures are reported in cubic and orthorhombic lattices at 1.92 and 2.36 Å resolution, respectively. This MCO forms trimers similar to those found in other two‐domain MCOs, but is unique in forming a higher order dodecameric structure.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 National Cancer Institute (NCI) US Department of Education AC02-06CH11357; ACB-12002; AGM-12006; P30GM138396; P015B180101-21 USDOE Office of Science (SC), Basic Energy Sciences (BES) National Institutes of Health (NIH)
ISSN:	2059-7983 0907-4449 2059-7983 1399-0047
DOI:	10.1107/S205979832100944X