7NED
Thiourocanate hydratase from Paenibacillus sp. Soil724D2 in complex with cofactor NAD+ and urocanate
Summary for 7NED
| Entry DOI | 10.2210/pdb7ned/pdb |
| Descriptor | Urocanate hydratase, (2E)-3-(1H-IMIDAZOL-4-YL)ACRYLIC ACID, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | lyase, thiourocanate hydratase, ergothioneine catabolism |
| Biological source | Paenibacillus sp. Soil724D2 |
| Total number of polymer chains | 1 |
| Total formula weight | 61130.72 |
| Authors | Leisinger, F.,Seebeck, F.P. (deposition date: 2021-02-03, release date: 2021-02-24, Last modification date: 2024-01-31) |
| Primary citation | Beliaeva, M.A.,Leisinger, F.,Seebeck, F.P. In Vitro Reconstitution of a Five-Step Pathway for Bacterial Ergothioneine Catabolism. Acs Chem.Biol., 16:397-403, 2021 Cited by PubMed Abstract: Ergothioneine is a histidine-derived sulfur metabolite that is biosynthesized by bacteria and fungi. Plants and animals absorb ergothioneine as a micronutrient from their environment or nutrition. Several different mechanisms of microbial ergothioneine production have been described in the past ten years. Much less is known about the genetic and structural basis for ergothioneine catabolism. In this report, we describe the reconstitution of a five-step pathway that degrades ergothioneine to l-glutamate, trimethylamine, hydrogen sulfide, carbon dioxide, and ammonia. The first two steps are catalyzed by the two enzymes ergothionase and thiourocanate hydratase. These enzymes are closely related to the first two enzymes in histidine catabolism. However, the crystal structure of thiourocanate hydratase from the firmicute reveals specific structural features that strictly differentiate the activity of this enzyme from that of urocanate hydratases. The final two steps are catalyzed by metal-dependent hydrolases that share most homology with the last two enzymes in uracil catabolism. The early and late part of this pathway are connected by an entirely new enzyme type that catalyzes desulfurization of a thiohydantoin intermediate. Homologous enzymes are encoded in many soil-dwelling firmicutes and proteobacteria, suggesting that bacterial activity may have a significant impact on the environmental availability of ergothioneine. PubMed: 33544568DOI: 10.1021/acschembio.0c00968 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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