4P6S

Crystal Structure of tyrosinase from Bacillus megaterium with L-DOPA in the active site

4P6S の概要

• エントリーDOI: 10.2210/pdb4p6s/pdb
• 関連するPDBエントリー: 4P6R 4P6T
• 分子名称: Tyrosinase, ZINC ION, 3,4-DIHYDROXYPHENYLALANINE, ... (4 entities in total)
• 機能のキーワード: l-dopa, type 3 copper proteins, oxidoreductase
• 由来する生物種: Bacillus megaterium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67759.74

構造登録者

Goldfeder, M.,Kanteev, M.,Adir, N.,Fishman, A. (登録日: 2014-03-25, 公開日: 2014-07-30, 最終更新日: 2023-12-27)

主引用文献

Goldfeder, M.,Kanteev, M.,Isaschar-Ovdat, S.,Adir, N.,Fishman, A.
Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins.
Nat Commun, 5:4505-4505, 2014

PubMed Abstract: Tyrosinase is responsible for the two initial enzymatic steps in the conversion of tyrosine to melanin. Many tyrosinase mutations are the leading cause of albinism in humans, and it is a prominent biotechnology and pharmaceutical industry target. Here we present crystal structures that show that both monophenol hydroxylation and diphenol oxidation occur at the same site. It is suggested that concurrent presence of a phenylalanine above the active site and a restricting thioether bond on the histidine coordinating CuA prevent hydroxylation of monophenols by catechol oxidases. Furthermore, a conserved water molecule activated by E195 and N205 is proposed to mediate deprotonation of the monophenol at the active site. Overall, the structures reveal precise steps in the enzymatic catalytic cycle as well as differences between tyrosinases and other type-3 copper enzymes.

PubMed: 25074014
DOI: 10.1038/ncomms5505

実験手法

X-RAY DIFFRACTION (2.2 Å)