6JUA
Aspergillus oryzae pro-tyrosinase oxygen-bound C92A mutant
Summary for 6JUA
| Entry DOI | 10.2210/pdb6jua/pdb |
| Descriptor | Tyrosinase, COPPER (II) ION, PEROXIDE ION, ... (4 entities in total) |
| Functional Keywords | tyrosinase, copper enzyme, dinuclear copper center, oxidoreductase |
| Biological source | Aspergillus oryzae (Yellow koji mold) |
| Total number of polymer chains | 2 |
| Total formula weight | 142951.22 |
| Authors | Fujieda, N.,Umakoshi, K.,Nishikawa, Y.,Kurisu, G.,Itoh, S. (deposition date: 2019-04-13, release date: 2020-05-13, Last modification date: 2023-11-22) |
| Primary citation | 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 Cited by 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: 32356371DOI: 10.1002/anie.202004733 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report
