4zfj | pdb_00004zfj

Ergothioneine-biosynthetic Ntn hydrolase EgtC, apo form

spinqualitylabelsall models 4zfj, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zfj is a 12 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: MES, MSE, XPE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EGTC_MYCS2 Catalyzes the hydrolysis of the gamma-glutamyl amide bond from N-(gamma-glutamyl)-[N(alpha),N(alpha),N(alpha)-trimethyl-L-histidinyl]-cysteine sulfoxide to produce hercynylcysteine sulfoxide. Publication Abstract from PubMed The ubiquitous sulfur metabolite ergothioneine is biosynthesized by oxidative attachment of a sulfur atom to the imidazole ring of Nalpha-trimethylhistidine. Most actinobacteria, including Mycobacterium tuberculosis, use gamma-glutamyl cysteine as a sulfur donor. In subsequent steps the carbon scaffold of gamma-glutamyl cysteine is removed by the glutamine amidohydrolase EgtC and the beta-lyase EgtE. We determined the crystal structure of EgtC from Mycobacterium smegmatis in complex with its physiological substrate. The set of active site residues that define substrate specificity in EgtC are highly conserved, even in homologues that are not involved in ergothioneine production. This conservation is compounded by the phylogenetic distribution of EgtC-like enzymes indicates that their last common ancestor might have emerged for a purpose other than ergothioneine production. Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC.,Vit A, Mashabela GT, Blankenfeldt W, Seebeck FP Chembiochem. 2015 Jun 16. doi: 10.1002/cbic.201500168. PMID:26079795 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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