8qfo | pdb_00008qfo

Ergothioneine dioxygenase, variant Y128F, from Thermocatellispora tengchongensis in complex with manganese

spinqualitylabelsall models 8qfo, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8qfo is a 2 chain structure with sequence from Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: ACT, MG, MN, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A840P3H4_9ACTN Publication Abstract from PubMed 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 or hydrogen peroxide, and may therefore protect cells against oxidative stress. In this report 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 Na-trimethylhistidine and SO2. The discovery that certain actinobacteria contain the enzymatic machinery for O2-dependent biosynthesis and O2-dependent degradation of ergothioneine indicates that these organisms may actively manage their ergothioneine content. Enzyme-Catalyzed Oxidative Degradation of Ergothioneine.,Nalivaiko E, Vasseur CM, Seebeck FP Angew Chem Int Ed Engl. 2023 Dec 14:e202318445. doi: 10.1002/anie.202318445. PMID:38095354 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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