7RAC
Crystal structure of a dodecameric multicopper oxidase from M. hydrothermalis in an orthorhombic lattice
Summary for 7RAC
| Entry DOI | 10.2210/pdb7rac/pdb |
| Descriptor | multicopper oxidase, (4S)-2-METHYL-2,4-PENTANEDIOL, COPPER (II) ION, ... (5 entities in total) |
| Functional Keywords | multicopper oxidase thermophile dodecamer laccase, oxidoreductase |
| Biological source | Marinithermus hydrothermalis |
| Total number of polymer chains | 12 |
| Total formula weight | 477903.53 |
| Authors | Georgiadis, M.M.,Ogata, C.M. (deposition date: 2021-06-30, release date: 2021-10-20, Last modification date: 2024-04-03) |
| Primary citation | Paavola, J.L.,Battistin, U.,Ogata, C.M.,Georgiadis, M.M. Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis. Acta Crystallogr D Struct Biol, 77:1336-1345, 2021 Cited by PubMed Abstract: 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. PubMed: 34605435DOI: 10.1107/S205979832100944X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.36 Å) |
Structure validation
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