3AWW

Crystal structure of Streptomyces tyrosinase in a complex with caddie soaked in a Cu(II)-containing solution for 80 hr: occupancy of CuA is high

3AWW の概要

• エントリーDOI: 10.2210/pdb3aww/pdb
• 関連するPDBエントリー: 3AWS 3AWT 3AWU 3AWV 3AWX 3AWY 3AWZ 3AX0
• 分子名称: Tyrosinase, MelC, 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, 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: 46743.42

構造登録者

Matoba, Y.,Sugiyama, M. (登録日: 2011-03-26, 公開日: 2011-06-29, 最終更新日: 2023-11-01)

主引用文献

Matoba, Y.,Bando, N.,Oda, K.,Noda, M.,Higashikawa, F.,Kumagai, T.,Sugiyama, M.
A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein
J.Biol.Chem., 286:30219-30231, 2011

PubMed Abstract: The Cu(II)-soaked crystal structure of tyrosinase that is present in a complex with a protein, designated "caddie," which we previously determined, possesses two copper ions at its catalytic center. We had identified two copper-binding sites in the caddie protein and speculated that copper bound to caddie may be transported to the tyrosinase catalytic center. In our present study, at a 1.16-1.58 Å resolution, we determined the crystal structures of tyrosinase complexed with caddie prepared by altering the soaking time of the copper ion and the structures of tyrosinase complexed with different caddie mutants that display little or no capacity to activate tyrosinase. Based on these structures, we propose a molecular mechanism by which two copper ions are transported to the tyrosinase catalytic center with the assistance of caddie acting as a metallochaperone.

PubMed: 21730070
DOI: 10.1074/jbc.M111.256818

実験手法

X-RAY DIFFRACTION (1.35 Å)