edoc

An Alternative Active Site Architecture for O2 Activation in the Ergothioneine Biosynthetic EgtB from Chloracidobacterium thermophilum

Stampfli, Anja R. and Goncharenko, Kristina V. and Meury, Marcel and Dubey, Badri N. and Schirmer, Tilman and Seebeck, Florian P.. (2019) An Alternative Active Site Architecture for O2 Activation in the Ergothioneine Biosynthetic EgtB from Chloracidobacterium thermophilum. Journal of American Chemical Society, 141 (13). 5275-5285 .

[img] PDF - Accepted Version
Restricted to Repository staff only until 18 March 2020.

14Mb

Official URL: https://edoc.unibas.ch/70088/

Downloads: Statistics Overview

Abstract

Sulfoxide synthases are nonheme iron enzymes that catalyze oxidative carbon-sulfur bond formation between cysteine derivatives and N-α-trimethylhistidine as a key step in the biosynthesis of thiohistidines. The complex catalytic mechanism of this enzyme reaction has emerged as the controversial subject of several biochemical and computational studies. These studies all used the structure of the γ-glutamyl cysteine utilizing sulfoxide synthase, MthEgtB from Mycobacterium thermophilum (EC 1.14.99.50), as a structural basis. To provide an alternative model system, we have solved the crystal structure of CthEgtB from Chloracidobacterium thermophilum (EC 1.14.99.51) that utilizes cysteine as a sulfur donor. This structure reveals a completely different configuration of active site residues that are involved in oxygen binding and activation. Furthermore, comparison of the two EgtB structures enables a classification of all ergothioneine biosynthetic EgtBs into five subtypes, each characterized by unique active-site features. This active site diversity provides an excellent platform to examine the catalytic mechanism of sulfoxide synthases by comparative enzymology, but also raises the question as to why so many different solutions to the same biosynthetic problem have emerged.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Schirmer)
05 Faculty of Science > Departement Chemie > Chemie > Molecular Bionics (Seebeck)
UniBasel Contributors:Goncharenko, Kristina and Meury, Marcel and Dubey, Badri Nath and Schirmer, Tilman and Seebeck, Florian Peter and Stampfli, Anja
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
ISSN:0002-7863
e-ISSN:1520-5126
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Related URLs:
Identification Number:
Last Modified:25 Jun 2019 08:47
Deposited On:25 Jun 2019 08:47

Repository Staff Only: item control page