6ELS
Structure of latent apple tyrosinase (MdPPO1)
Summary for 6ELS
| Entry DOI | 10.2210/pdb6els/pdb |
| Descriptor | Polyphenol oxidase, chloroplastic, COPPER (II) ION, OXYGEN ATOM, ... (4 entities in total) |
| Functional Keywords | polyphenol oxidase, tyrosinase, latent form, oxidoreductase |
| Biological source | Malus domestica (Apple) |
| Total number of polymer chains | 1 |
| Total formula weight | 56664.17 |
| Authors | Kampatsikas, I.,Bijelic, A.,Pretzler, M.,Rompel, A. (deposition date: 2017-09-29, release date: 2019-03-20, Last modification date: 2024-05-01) |
| Primary citation | Kampatsikas, I.,Bijelic, A.,Pretzler, M.,Rompel, A. A Peptide-Induced Self-Cleavage Reaction Initiates the Activation of Tyrosinase. Angew.Chem.Int.Ed.Engl., 58:7475-7479, 2019 Cited by PubMed Abstract: The conversion of inactive pro-polyphenol oxidases (pro-PPOs) into the active enzyme results from the proteolytic cleavage of its C-terminal domain. Herein, a peptide-mediated cleavage process that activates pro-MdPPO1 (Malus domestica) is reported. Mass spectrometry, mutagenesis studies, and X-ray crystal-structure analysis of pro-MdPPO1 (1.35 Å) and two separated C-terminal domains, one obtained upon self-cleavage of pro-MdPPO1 and the other one produced independently, were applied to study the observed self-cleavage. The sequence Lys 355-Val 370 located in the linker between the active and the C-terminal domain is indispensable for the self-cleavage. Partial introduction (Lys 352-Ala 360) of this peptide into the sequence of two other PPOs, MdPPO2 and aurone synthase (CgAUS1), triggered self-cleavage in the resulting mutants. This is the first experimental proof of a self-cleavage-inducing peptide in PPOs, unveiling a new mode of activation for this enzyme class that is independent of any external protease. PubMed: 30825403DOI: 10.1002/anie.201901332 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.346 Å) |
Structure validation
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