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

ABSTRACT: 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.

SUBMITTER: Weiss AKH

PROVIDER: S-EPMC7056447 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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

Weiss Alexander K H AKH Naschberger Andreas A Cappuccio Elia E Metzger Christina C Mottes Lorenza L Holzknecht Max M von Velsen Jill J Bowler Matthew W MW Rupp Bernhard B Jansen-Dürr Pidder P

Bioscience reports 20200301 3

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 recognize ...[more]

PMID: 32068790

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