Department of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul, 08826, Republic of Korea.
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul, 08826, Republic of Korea.
Sci Rep. 2024 Feb 15;14(1):3819. doi: 10.1038/s41598-024-54205-7.
Formate dehydrogenase (FDH) is critical for the conversion between formate and carbon dioxide. Despite its importance, the structural complexity of FDH and difficulties in the production of the enzyme have made elucidating its unique physicochemical properties challenging. Here, we purified recombinant Methylobacterium extorquens AM1 FDH (MeFDH1) and used cryo-electron microscopy to determine its structure. We resolved a heterodimeric MeFDH1 structure at a resolution of 2.8 Å, showing a noncanonical active site and a well-embedded Fe-S redox chain relay. In particular, the tungsten bis-molybdopterin guanine dinucleotide active site showed an open configuration with a flexible C-terminal cap domain, suggesting structural and dynamic heterogeneity in the enzyme.
甲酸脱氢酶（FDH）在甲酸和二氧化碳之间的转化中起着关键作用。尽管它很重要，但 FDH 的结构复杂性和酶的生产困难使得阐明其独特的物理化学性质具有挑战性。在这里，我们纯化了重组甲基杆菌外消旋 AM1 FDH（MeFDH1），并使用低温电子显微镜确定了它的结构。我们以 2.8Å 的分辨率解析了一个异源二聚体 MeFDH1 结构，显示了一个非典型的活性位点和一个良好嵌入的 Fe-S 氧化还原链接力。特别是，钨双钼喋呤鸟嘌呤二核苷酸活性位点显示出开放的构象，带有一个灵活的 C 端帽结构域，表明酶的结构和动态异质性。
