2Q9O

Near-atomic resolution structure of a Melanocarpus albomyces laccase

2Q9O の概要

• エントリーDOI: 10.2210/pdb2q9o/pdb
• 関連するPDBエントリー: 1gw0 2ih8 2ih9
• 分子名称: Laccase-1, GLYCEROL, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• 機能のキーワード: laccase, multicopper oxidase, melanocarpus albomyces, 2-oxohistidine, oxidoreductase
• 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: 131833.93

構造登録者

Hakulinen, N.,Rouvinen, J. (登録日: 2007-06-13, 公開日: 2008-03-25, 最終更新日: 2025-03-26)

主引用文献

Hakulinen, N.,Andberg, M.,Kallio, J.,Koivula, A.,Kruus, K.,Rouvinen, J.
A near atomic resolution structure of a Melanocarpus albomyces laccase.
J.Struct.Biol., 162:29-39, 2008

PubMed Abstract: We have solved a crystal structure from Melanocarpus albomyces laccase expressed in the filamentous fungus Trichoderma reesei (rMaL) at 1.3A resolution by using synchrotron radiation at 100K. At the moment, this is the highest resolution that has been attained for any multicopper oxidase. The present structure confirmed our earlier proposal regarding the dynamic behaviour of the copper cluster. Thermal ellipsoids of copper atoms indicated movements of trinuclear site coppers. The direction of the type-3 copper motion was perpendicular to the type-2 copper. In addition, the structure at 1.3A resolution allowed us to describe important solvent cavities of the enzyme and the structure is also compared with other known multicopper oxidases. T2 and T3 solvent cavities, and a putative SDS-gate, formed by Ser142, Ser510 and the C-terminal Asp556 of rMaL, are described. We also observed a 2-oxohistidine, an oxidized histidine, possibly caused by a metal-catalysed oxidation by the trinuclear site coppers. To our knowledge, this is the first time that 2-oxohistidine has been observed in a protein crystal structure.

PubMed: 18249560
DOI: 10.1016/j.jsb.2007.12.003

実験手法

X-RAY DIFFRACTION (1.3 Å)