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Structure of the Sulfoxide Synthase EgtB from the Ergothioneine Biosynthetic Pathway

Goncharenko, Kristina V. and Vit, Allegra and Blankenfeldt, Wulf and Seebeck, Florian P.. (2015) Structure of the Sulfoxide Synthase EgtB from the Ergothioneine Biosynthetic Pathway. Angewandte Chemie International Edition, 54 (9). pp. 2821-2824.

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Official URL: http://edoc.unibas.ch/dok/A6348318

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Abstract

The non-heme iron enzyme EgtB catalyzes O2 -dependent C-S bond formation between γ-glutamyl cysteine and N-α-trimethyl histidine as the central step in ergothioneine biosynthesis. Both, the catalytic activity and the architecture of EgtB are distinct from known sulfur transferases or thiol dioxygenases. The crystal structure of EgtB from Mycobacterium thermoresistibile in complex with γ-glutamyl cysteine and N-α-trimethyl histidine reveals that the two substrates and three histidine residues serve as ligands in an octahedral iron binding site. This active site geometry is consistent with a catalytic mechanism in which C-S bond formation is initiated by an iron(III)-complexed thiyl radical attacking the imidazole ring of N-α-trimethyl histidine.
Faculties and Departments:05 Faculty of Science
05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Molecular Bionics (Seebeck)
UniBasel Contributors:Seebeck, Florian Peter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:1433-7851
e-ISSN:1521-3773
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:23 Oct 2019 12:57
Deposited On:10 Apr 2015 09:12

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