2ZMX

Crystal structure of the met1-form of the copper-bound tyrosinase in complex with a caddie protein from Streptomyces castaneoglobisporus obtained by soaking in cupric sulfate solution for 36 hours

「1WX3」から置き換えられました

2ZMX の概要

• エントリーDOI: 10.2210/pdb2zmx/pdb
• 関連するPDBエントリー: 2ZMY 2ZMZ 2ZN0 2ZN1 2ZN2 2ZN3 2ZN4 2ZN5 2ZN6
• 分子名称: Tyrosinase, CADDIE, COPPER (II) ION, ... (5 entities in total)
• 機能のキーワード: tyrosinase, binary complex, type-3 copper, dioxygen, copper transfer, oxidoreductase-metal transport complex, copper, metal-binding, oxidoreductase/metal transport
• 由来する生物種: Streptomyces castaneoglobisporus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46857.58

構造登録者

Matoba, Y.,Sugiyama, M. (登録日: 2008-04-21, 公開日: 2009-04-07, 最終更新日: 2023-11-01)

主引用文献

Matoba, Y.,Kumagai, T.,Yamamoto, A.,Yoshitsu, H.,Sugiyama, M.
Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible during Catalysis
J.Biol.Chem., 281:8981-8990, 2006

PubMed Abstract: At high resolution, we determined the crystal structures of copper-bound and metal-free tyrosinase in a complex with ORF378 designated as a "caddie" protein because it assists with transportation of two CuII ions into the tyrosinase catalytic center. These structures suggest that the caddie protein covers the hydrophobic molecular surface of tyrosinase and interferes with the binding of a substrate tyrosine to the catalytic site of tyrosinase. The caddie protein, which consists of one six-strandedbeta-sheet and one alpha-helix, has no similarity with all proteins deposited into the Protein Data Bank. Although tyrosinase and catechol oxidase are classified into the type 3 copper protein family, the latter enzyme lacks monooxygenase activity. The difference in catalytic activity is based on the structural observations that a large vacant space is present just above the active center of tyrosinase and that one of the six His ligands for the two copper ions is highly flexible. These structural characteristics of tyrosinase suggest that, in the reaction that catalyzes the ortho-hydroxylation of monophenol, one of the two Cu(II) ions is coordinated by the peroxide-originated oxygen bound to the substrate. Our crystallographic study shows evidence that the tyrosinase active center formed by dinuclear coppers is flexible during catalysis.

PubMed: 16436386
DOI: 10.1074/jbc.M509785200

実験手法

X-RAY DIFFRACTION (1.33 Å)