6s7j

Native crystal structure of ergothioneine degrading enzyme Ergothionase from Treponema denticola

spinqualitylabelsall models 6s7j, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6s7j is a 8 chain structure with sequence from Treponema denticola sp33. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: HMPREF9733_00339 (Treponema denticola SP33) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Ergothioneine is a sulfur-containing histidine derivative that emerges from microbial biosynthesis and enters the human body through intestinal uptake and regulated distribution into specific tissues. Although the proteins involved in biosynthesis and uptake are well characterized, less is known about the degradative pathways of ergothioneine. This report describes the crystal structure of the active form of ergothionase from the oral pathogen Treponema denticola complexed with the substrate analogue desmethyl-ergothioneine sulfonic acid. This enzyme catalyzes the 1,2-elimination of trimethylamine from ergothioneine and ergothioneine sulfonic acid by using a unique mode of substrate activation combined with acid/base catalysis. This structural and mechanistic investigation revealed four essential catalytic residues, which are strictly conserved in homologous proteins from common gastrointestinal bacteria and numerous pathogenic bacteria, suggesting that bacterial activity may play an important role in determining the availability of ergothioneine in healthy and diseased human tissue. Structure and Mechanism of Ergothionase from Treponema denticola.,Maurer A, Leisinger F, Lim D, Seebeck FP Chemistry. 2019 Jun 12. doi: 10.1002/chem.201901866. PMID:31188501 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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