4JHU

T2-depleted laccase from Coriolopsis caperata soaked with CuCl

4JHU の概要

• エントリーDOI: 10.2210/pdb4jhu/pdb
• 関連するPDBエントリー: 4JHV
• 分子名称: LACCASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (5 entities in total)
• 機能のキーワード: beta sheet, 4-copper protein, metal-binding, oxidoreductase, laccase
• 由来する生物種: Coriolopsis Caperata
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55303.70

構造登録者

Polyakov, K.M.,Fedorova, T.V.,Glazunova, O.A.,Kurzeev, S.A.,Maloshenok, L.G.,Koroleva, O.A. (登録日: 2013-03-05, 公開日: 2014-04-23, 最終更新日: 2024-11-20)

主引用文献

Glazunova, O.A.,Polyakov, K.M.,Fedorova, T.V.,Dorovatovskii, P.V.,Koroleva, O.V.
Elucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions.
Acta Crystallogr.,Sect.D, 71:854-861, 2015

PubMed Abstract: Laccases are members of a large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. A new laccase was isolated from the basidiomycete Coriolopsis caperata strain 0677 and its amino-acid sequence was determined. According to its physicochemical properties and spectroscopic features, the laccase from C. caperata is a high redox-potential blue laccase. Attempts to crystallize the native enzyme were unsuccessful. The copper type 2-depleted (T2D) laccase was prepared and crystallized. The structure of T2D laccase from C. caperata was solved at 1.6 Å resolution, and attempts to reconstruct the T2 copper centre were performed using Cu(+) and Cu(2+) ions. The structure of T2D+Cu(+) laccase was solved at 1.89 Å resolution. It was shown that the T2D+Cu(+) laccase structure contained four copper ions in the active site. Reconstruction could not be achieved when the T2D laccase crystals were treated with CuSO4.

PubMed: 25849396
DOI: 10.1107/S1399004715001595

実験手法

X-RAY DIFFRACTION (1.89 Å)