4X8D

Ergothioneine-biosynthetic sulfoxide synthase EgtB in complex with N,N-dimethyl-histidine and gamma-glutamyl-cysteine

Summary for 4X8D

• Entry DOI: 10.2210/pdb4x8d/pdb
• Related: 4X8B 4X8E
• Descriptor: Sulfoxide synthase EgtB, GAMMA-GLUTAMYLCYSTEINE, N,N-dimethyl-L-histidine, ... (9 entities in total)
• Functional Keywords: sulfoxide synthase, ergothioneine biosynthesis, c-lectin, dinb, non-heme fe(ii) enzyme, oxidoreductase
• Biological source: Mycobacterium thermoresistibile ATCC 19527
• Total number of polymer chains: 2
• Total formula weight: 100869.80

Authors

Vit, A.,Goncharenko, K.V.,Blankenfeldt, W.,Seebeck, F.P. (deposition date: 2014-12-10, release date: 2015-01-28, Last modification date: 2024-11-13)

Primary citation

Goncharenko, K.V.,Vit, A.,Blankenfeldt, W.,Seebeck, F.P.
Structure of the Sulfoxide Synthase EgtB from the Ergothioneine Biosynthetic Pathway.
Angew.Chem.Int.Ed.Engl., 54:2821-2824, 2015

PubMed 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.

PubMed: 25597398
DOI: 10.1002/anie.201410045

Experimental method

X-RAY DIFFRACTION (1.98 Å)