人源和鼠源富马酰乙酰乙酸酶蛋白 1 的结构与功能比较
Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse.
机构信息
University of Innsbruck, Research Institute for Biomedical Aging Research, Rennweg 10, Innsbruck A-6020, Austria.
University of Innsbruck, Center for Molecular Biosciences Innsbruck (CMBI), Innrain 80-82, Innsbruck A-6020, Austria.
出版信息
Biosci Rep. 2020 Mar 27;40(3). doi: 10.1042/BSR20194431.
FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.
FAH 结构域包含蛋白 1（FAHD1）是一种哺乳动物线粒体蛋白，具有酰基辅酶 A 水解酶（ApH）和草酰乙酸脱羧酶（ODx）的双重活性。我们报告了小鼠 FAHD1 的晶体结构和小鼠 FAHD1 活性位点的结构映射。尽管与人类 FAHD1 具有高度的结构相似性，但我们能够产生一种能够识别小鼠 FAHD1 但不能识别人类形式的兔单克隆抗体（RabMab），而多克隆抗体则可以识别两种蛋白质。表位作图结合我们已提交的晶体结构揭示，该表位与报道的小鼠 FAHD1 中的 SIRT3 去乙酰化位点重叠。
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