4CZO

Crystal structure of the extralong fungal manganese peroxidase from Ceriporiopsis subvermispora in complex with manganese

4CZO の概要

• エントリーDOI: 10.2210/pdb4czo/pdb
• 関連するPDBエントリー: 4CZN 4CZP 4CZQ 4CZR
• 分子名称: EXTRALONG MANGANESE PEROXIDASE, CALCIUM ION, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: class ii (fungal) peroxidases, protoporphyrin ix, electron transfer, lignin peroxidase, lignin degradation, manganese peroxidase, mnii oxidation, peroxidase, oxidoreductase, hydrogen peroxide, iron, manganese, metal-binding, secreted
• 由来する生物種: CERIPORIOPSIS SUBVERMISPORA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39553.67

構造登録者

Medrano, F.J.,Romero, A. (登録日: 2014-04-21, 公開日: 2014-12-10, 最終更新日: 2024-11-06)

主引用文献

Fernandez-Fueyo, E.,Acebes, S.,Ruiz-Duenas, F.J.,Martinez, M.J.,Romero, A.,Medrano, F.J.,Guallar, V.,Martinez, A.T.
Structural Implications of the C-Terminal Tail in the Catalytic and Stability Properties of Manganese Peroxidases from Ligninolytic Fungi
Acta Crystallogr.,Sect.D, 70:3253-, 2014

PubMed Abstract: The genome of Ceriporiopsis subvermispora includes 13 manganese peroxidase (MnP) genes representative of the three subfamilies described in ligninolytic fungi, which share an Mn(2+)-oxidation site and have varying lengths of the C-terminal tail. Short, long and extralong MnPs were heterologously expressed and biochemically characterized, and the first structure of an extralong MnP was solved. Its C-terminal tail surrounds the haem-propionate access channel, contributing to Mn(2+) oxidation by the internal propionate, but prevents the oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS), which is only oxidized by short MnPs and by shortened-tail variants from site-directed mutagenesis. The tail, which is anchored by numerous contacts, not only affects the catalytic properties of long/extralong MnPs but is also associated with their high acidic stability. Cd(2+) binds at the Mn(2+)-oxidation site and competitively inhibits oxidation of both Mn(2+) and ABTS. Moreover, mutations blocking the haem-propionate channel prevent substrate oxidation. This agrees with molecular simulations that position ABTS at an electron-transfer distance from the haem propionates of an in silico shortened-tail form, while it cannot reach this position in the extralong MnP crystal structure. Only small differences exist between the long and the extralong MnPs, which do not justify their classification as two different subfamilies, but they significantly differ from the short MnPs, with the presence/absence of the C-terminal tail extension being implicated in these differences.

PubMed: 25478843
DOI: 10.1107/S1399004714022755

実験手法

X-RAY DIFFRACTION (1.199 Å)