1GW0

Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form

1GW0 の概要

• エントリーDOI: 10.2210/pdb1gw0/pdb
• 分子名称: LACCASE-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (12 entities in total)
• 機能のキーワード: oxidoreductase, laccase, multi-copper oxidases, oxygen reduction, ascomycete, c-terminal plug
• 由来する生物種: MELANOCARPUS ALBOMYCES
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 132160.26

構造登録者

Hakulinen, N.,Kiiskinen, L.-L.,Kruus, K.,Saloheimo, M.,Koivula, A.,Rouvinen, J. (登録日: 2002-03-01, 公開日: 2002-07-31, 最終更新日: 2024-11-13)

主引用文献

Hakulinen, N.,Kiiskinen, L.-L.,Kruus, K.,Saloheimo, M.,Paananen, A.,Koivula, A.,Rouvinen, J.
Crystal Structure of a Laccase from Melanocarpus Albomyces with an Intact Trinuclear Copper Site
Nat.Struct.Biol., 9:601-605, 2002

PubMed Abstract: We have crystallized the ascomycete laccase from Melanocarpus albomyces with all four coppers present and determined the crystal structure at 2.4 A resolution. The enzyme is heavily glycosylated and consists of three cupredoxin-like domains, similar to those found in the Cu-depleted basidiomycete laccase from Coprinus cinereus. However, there are significant differences in the loops forming the substrate-binding pocket. In addition, the crystal structure of the M. albomyces laccase revealed elongated electron density between all three coppers in the trinuclear copper site, suggesting that an oxygen molecule binds with a novel geometry. This oxygen, required in the reaction, may enter the trinuclear site through the tunnel, which is open in the structure of the C. cinereus laccase. In contrast, the C-terminus on the M. albomyces laccase forms a plug that blocks this access.

PubMed: 12118243
DOI: 10.1038/NSB823

実験手法

X-RAY DIFFRACTION (2.4 Å)