6T86
Urocanate reductase in complex with FAD
6T86 の概要
| エントリーDOI | 10.2210/pdb6t86/pdb |
| 分子名称 | Urocanate reductase, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (7 entities in total) |
| 機能のキーワード | urocanate reductase, bacterial enzyme, oxidoreductase |
| 由来する生物種 | Shewanella oneidensis (strain MR-1) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 51752.08 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.56 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






