4x8e

Ergothioneine-biosynthetic sulfoxide synthase EgtB in complex with N,N,N-trimethyl-histidine

spinqualitylabelsall models 4x8e, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4x8e is a 2 chain structure with sequence from Mycolicibacterium thermoresistibile ATCC 19527. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: AVJ, CA, CL, FE, GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EGTB_MYCT3 Catalyzes the oxidative sulfurization of hercynine (N-alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine. Publication Abstract from PubMed The non-heme iron enzyme EgtB catalyzes O2 -dependent CS bond formation between gamma-glutamyl cysteine and N-alpha-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 gamma-glutamyl cysteine and N-alpha-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 CS bond formation is initiated by an iron(III)-complexed thiyl radical attacking the imidazole ring of N-alpha-trimethyl histidine. Structure of the Sulfoxide Synthase EgtB from the Ergothioneine Biosynthetic Pathway.,Goncharenko KV, Vit A, Blankenfeldt W, Seebeck FP Angew Chem Int Ed Engl. 2015 Jan 16. doi: 10.1002/anie.201410045. PMID:25597398 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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