8QFQ

Ergothioneine dioxygenase, variant H147A, from Thermocatellispora tengchongensis in complex with manganese

Summary for 8QFQ

• Entry DOI: 10.2210/pdb8qfq/pdb
• Descriptor: Cysteine dioxygenase, MANGANESE (II) ION, TRIETHYLENE GLYCOL, ... (7 entities in total)
• Functional Keywords: thiol dioxygenase ergothioneine dioxygenase, oxidoreductase
• Biological source: Thermocatellispora tengchongensis
• Total number of polymer chains: 2
• Total formula weight: 41977.62

Authors

Vasseur, C.M.,Seebeck, F.P. (deposition date: 2023-09-04, release date: 2023-12-27, Last modification date: 2024-03-27)

Primary citation

Nalivaiko, E.Y.,Vasseur, C.M.,Seebeck, F.P.
Enzyme-Catalyzed Oxidative Degradation of Ergothioneine.
Angew.Chem.Int.Ed.Engl., 63:e202318445-e202318445, 2024

PubMed Abstract: Ergothioneine is a sulfur-containing metabolite that is produced by bacteria and fungi, and is absorbed by plants and animals as a micronutrient. Ergothioneine reacts with harmful oxidants, including singlet oxygen and hydrogen peroxide, and may therefore protect cells against oxidative stress. Herein we describe two enzymes from actinobacteria that cooperate in the specific oxidative degradation of ergothioneine. The first enzyme is an iron-dependent thiol dioxygenase that produces ergothioneine sulfinic acid. A crystal structure of ergothioneine dioxygenase from Thermocatellispora tengchongensis reveals many similarities with cysteine dioxygenases, suggesting that the two enzymes share a common mechanism. The second enzyme is a metal-dependent ergothioneine sulfinic acid desulfinase that produces Nα-trimethylhistidine and SO . The discovery that certain actinobacteria contain the enzymatic machinery for O -dependent biosynthesis and O -dependent degradation of ergothioneine indicates that these organisms may actively manage their ergothioneine content.

PubMed: 38095354
DOI: 10.1002/anie.202318445

Experimental method

X-RAY DIFFRACTION (2.1 Å)