PDF(Pubmed)
Abstract：
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.
摘要：
甲酸脱氢酶(FDH)对于甲酸和二氧化碳之间的转化至关重要。尽管它很重要,FDH的结构复杂性和酶生产中的困难使得阐明其独特的理化性质具有挑战性。这里,我们纯化了重组甲基杆菌AM1FDH（MeFDH1），并使用低温电子显微镜确定其结构。我们以2.8µ的分辨率解析了异二聚体MeFDH1结构，显示出非规范活性位点和嵌入良好的Fe-S氧化还原链继电器。特别是,钨双钼蝶呤鸟嘌呤二核苷酸活性位点显示具有柔性C末端帽结构域的开放构型，表明酶的结构和动态异质性。
