Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse

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 hig...

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Detalles Bibliográficos
Autores principales: Weiss, Alexander K.H., Naschberger, Andreas, Cappuccio, Elia, Metzger, Christina, Mottes, Lorenza, Holzknecht, Max, von Velsen, Jill, Bowler, Matthew W., Rupp, Bernhard, Jansen-Dürr, Pidder
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2020
Materias:
Chemical Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7056447/
https://www.ncbi.nlm.nih.gov/pubmed/32068790
http://dx.doi.org/10.1042/BSR20194431
Descripción
Sumario: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.

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