6sbj | pdb_00006sbj

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

spinqualitylabelsall models 6sbj, resolution 2.22Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6sbj is a 4 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MG Gene: Fahd1, MNCb-4134 (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FAHD1_MOUSE] Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (By similarity). Also has oxaloacetate decarboxylase activity (PubMed:25575590).[UniProtKB:Q6P587] Publication Abstract from PubMed 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 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. Structural and Functional Comparison of Fumarylacetoacetate Domain Containing Protein 1 (FAHD1) in Human and Mouse.,Weiss AKH, Naschberger A, Cappuccio E, Metzger C, Mottes L, Holzknecht M, von Velsen J, Bowler MW, Rupp B, Jansen-Durr P Biosci Rep. 2020 Feb 18. pii: 222164. doi: 10.1042/BSR20194431. PMID:32068790 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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