7RAB

Crystal structure of a dodecameric multicopper oxidase from M. hydrothermalis in a cubic lattice

7RAB の概要

• エントリーDOI: 10.2210/pdb7rab/pdb
• 分子名称: multicopper oxidase, COPPER (II) ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: multicopper oxidase thermophile dodecamer laccase, oxidoreductase
• 由来する生物種: Marinithermus hydrothermalis
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 316609.36

構造登録者

Georgiadis, M.M. (登録日: 2021-06-30, 公開日: 2021-10-20, 最終更新日: 2024-04-03)

主引用文献

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

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: 34605435
DOI: 10.1107/S205979832100944X

実験手法

X-RAY DIFFRACTION (1.92 Å)