5YS9
Crystal structure of acyl-coA oxidase3 from Yarrowia lipolytica
Summary for 5YS9
| Entry DOI | 10.2210/pdb5ys9/pdb |
| Descriptor | Acyl-coenzyme A oxidase 3, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | fad-binding protein, oxidoreductase |
| Biological source | Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) |
| Cellular location | Peroxisome : O74936 |
| Total number of polymer chains | 2 |
| Total formula weight | 159918.41 |
| Authors | Kim, S.,Kim, K.-J. (deposition date: 2017-11-13, release date: 2018-02-28, Last modification date: 2023-11-22) |
| Primary citation | Kim, S.,Kim, K.J. Crystal Structure of Acyl-CoA Oxidase 3 fromYarrowia lipolyticawith Specificity for Short-Chain Acyl-CoA. J. Microbiol. Biotechnol., 28:597-605, 2018 Cited by PubMed Abstract: Acyl-CoA oxidases (ACOXs) play important roles in lipid metabolism, including peroxisomal fatty acid β-oxidation by the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The yeast can utilize fatty acids as a carbon source and thus has extensive biotechnological applications. The crystal structure of ACOX3 from (ACOX3) was determined at a resolution of 2.5 Å. It contained two molecules per asymmetric unit, and the monomeric structure was folded into four domains; Nα, Nβ, Cα1, and Cα2 domains. The cofactor flavin adenine dinucleotide was bound in the dimer interface. The substrate-binding pocket was located near the cofactor, and formed at the interface between the Nα, Nβ, and Cα1 domains. Comparisons with other ACOX structures provided structural insights into how ACOX has a substrate preference for short-chain acyl-CoA. In addition, the structure of ACOX3 was compared with those of medium- and long-chain ACOXs, and the structural basis for their differences in substrate specificity was discussed. PubMed: 29429324DOI: 10.4014/jmb.1711.11032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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