6T87
Urocanate reductase in complex with urocanate
Summary for 6T87
| Entry DOI | 10.2210/pdb6t87/pdb |
| Descriptor | Urocanate reductase, FLAVIN-ADENINE DINUCLEOTIDE, (2E)-3-(1H-IMIDAZOL-4-YL)ACRYLIC ACID, ... (8 entities in total) |
| Functional Keywords | urocanate reductase, bacterial enzyme, oxidoreductase |
| Biological source | Shewanella oneidensis (strain MR-1) |
| Total number of polymer chains | 1 |
| Total formula weight | 52123.10 |
| Authors | Venskutonyte, R.,Lindkvist-Petersson, K. (deposition date: 2019-10-24, release date: 2021-03-03, Last modification date: 2024-01-24) |
| Primary citation | Venskutonyte, R.,Koh, A.,Stenstrom, O.,Khan, M.T.,Lundqvist, A.,Akke, M.,Backhed, F.,Lindkvist-Petersson, K. Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production. Nat Commun, 12:1347-1347, 2021 Cited by PubMed Abstract: The human microbiome can produce metabolites that modulate insulin signaling. Type 2 diabetes patients have increased circulating concentrations of the microbially produced histidine metabolite, imidazole propionate (ImP) and administration of ImP in mice resulted in impaired glucose tolerance. Interestingly, the fecal microbiota of the patients had increased capacity to produce ImP, which is mediated by the bacterial enzyme urocanate reductase (UrdA). Here, we describe the X-ray structures of the ligand-binding domains of UrdA in four different states, representing the structural transitions along the catalytic reaction pathway of this unexplored enzyme linked to disease in humans. The structures in combination with functional data provide key insights into the mechanism of action of UrdA that open new possibilities for drug development strategies targeting type 2 diabetes. PubMed: 33649331DOI: 10.1038/s41467-021-21548-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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