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6SBJ

X-ray structure of mus musculus Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) apo-form uuncomplexed

Summary for 6SBJ
Entry DOI10.2210/pdb6sbj/pdb
DescriptorAcylpyruvase FAHD1, mitochondrial, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordshydrolase
Biological sourceMus musculus (Mouse)
Total number of polymer chains4
Total formula weight118010.52
Authors
Rupp, B.,Naschberger, A.,Weiss, A.K.H. (deposition date: 2019-07-21, release date: 2020-02-26, Last modification date: 2024-01-24)
Primary citationWeiss, A.K.H.,Naschberger, A.,Cappuccio, E.,Metzger, C.,Mottes, L.,Holzknecht, M.,von Velsen, J.,Bowler, M.W.,Rupp, B.,Jansen-Durr, P.
Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse.
Biosci.Rep., 40:-, 2020
Cited by
PubMed 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.
PubMed: 32068790
DOI: 10.1042/BSR20194431
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.22 Å)
Structure validation

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