6ELV

Recombinantly expressed C-terminal domain of MdPPO1 (Csole-domain)

Summary for 6ELV

• Entry DOI: 10.2210/pdb6elv/pdb
• Related: 6ELS 6ELT
• Descriptor: Polyphenol oxidase, chloroplastic, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: polyphenol oxidase, tyrosinase, c-temrinal domain, autolysis, oxidoreductase
• Biological source: Malus domestica (Apple)
• Total number of polymer chains: 1
• Total formula weight: 15836.54

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

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: 30825403
DOI: 10.1002/anie.201901332

Experimental method

X-RAY DIFFRACTION (1.05 Å)