5YS9

Crystal structure of acyl-coA oxidase3 from Yarrowia lipolytica

5YS9 の概要

• エントリーDOI: 10.2210/pdb5ys9/pdb
• 分子名称: Acyl-coenzyme A oxidase 3, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: fad-binding protein, oxidoreductase
• 由来する生物種: Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast)
• 細胞内の位置: Peroxisome : O74936
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 159918.41

構造登録者

Kim, S.,Kim, K.-J. (登録日: 2017-11-13, 公開日: 2018-02-28, 最終更新日: 2023-11-22)

主引用文献

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

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: 29429324
DOI: 10.4014/jmb.1711.11032

実験手法

X-RAY DIFFRACTION (2.5 Å)