6JU9

Aspergillus oryzae active-tyrosinase copper-bound C92A mutant complexed with L-tyrosine

6JU9 の概要

• エントリーDOI: 10.2210/pdb6ju9/pdb
• 分子名称: Tyrosinase, TYROSINE, 3,4-DIHYDROXYPHENYLALANINE, ... (6 entities in total)
• 機能のキーワード: tyrosinase, copper enzyme, dinuclear copper center, oxidoreductase
• 由来する生物種: Aspergillus oryzae (Yellow koji mold)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107867.46

構造登録者

Fujieda, N.,Umakoshi, K.,Nishikawa, Y.,Kurisu, G.,Itoh, S. (登録日: 2019-04-13, 公開日: 2020-05-13, 最終更新日: 2025-09-17)

主引用文献

Fujieda, N.,Umakoshi, K.,Ochi, Y.,Nishikawa, Y.,Yanagisawa, S.,Kubo, M.,Kurisu, G.,Itoh, S.
Copper-Oxygen Dynamics in the Tyrosinase Mechanism.
Angew.Chem.Int.Ed.Engl., 59:13385-13390, 2020

PubMed Abstract: The dinuclear copper enzyme, tyrosinase, activates O to form a (μ-η :η -peroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate. We herein report the near atomic resolution X-ray crystal structures of the active tyrosinases with substrate l-tyrosine. At their catalytic sites, CuA moved toward l-tyrosine (CuA1 → CuA2), whose phenol oxygen directly coordinates to CuA2, involving the movement of CuB (CuB1 → CuB2). The crystal structures and spectroscopic analyses of the dioxygen-bound tyrosinases demonstrated that the peroxide ligand rotated, spontaneously weakening its O-O bond. Thus, the copper migration induced by the substrate-binding is accompanied by rearrangement of the bound peroxide species so as to provide one of the peroxide oxygen atoms with access to the phenol substrate's ϵ carbon atom.

PubMed: 32356371
DOI: 10.1002/anie.202004733

実験手法

X-RAY DIFFRACTION (1.42 Å)