7Q86
Crystal structure of human peroxisomal acyl-Co-A oxidase 1a, FAD-bound-form
Summary for 7Q86
| Entry DOI | 10.2210/pdb7q86/pdb |
| Descriptor | Isoform 2 of Peroxisomal acyl-coenzyme A oxidase 1, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | acyl-co-a oxidase, peroxisomal enzyme, oxidoreductase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 153078.38 |
| Authors | Sonani, R.R.,Blat, A.,Dubin, G. (deposition date: 2021-11-10, release date: 2022-03-02, Last modification date: 2024-11-13) |
| Primary citation | Sonani, R.R.,Blat, A.,Dubin, G. Crystal structures of apo- and FAD-bound human peroxisomal acyl-CoA oxidase provide mechanistic basis explaining clinical observations. Int.J.Biol.Macromol., 205:203-210, 2022 Cited by PubMed Abstract: Peroxisomal acyl-CoA oxidase 1a (ACOX1a) catalyzes the first and rate-limiting step of fatty acid oxidation, the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The dysfunction of human ACOX1a (hACOX1a) leads to deterioration of the nervous system manifesting in myeloneuropathy, hypotonia and convulsions. Crystal structures of hACOX1a in apo- and cofactor (FAD)-bound forms were solved at 2.00 and 2.09 Å resolution, respectively. hACOX1a exists as a homo-dimer with solvation free energy gain (ΔG) of -44.7 kcal mol. Two FAD molecules bind at the interface of protein monomers completing the active sites. The substrate binding cleft of hACOX1a is wider compared to human mitochondrial very-long chain specific acyl-CoA dehydrogenase. Mutations (p.G178C, p.M278V and p.N237S) reported to cause dysfunctionality of hACOX1a are analyzed on its 3D-structure to understand structure-function related perturbations and explain the associated phenotypes. PubMed: 35149097DOI: 10.1016/j.ijbiomac.2022.02.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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