1WDK

fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native2)

1WDK の概要

• エントリーDOI: 10.2210/pdb1wdk/pdb
• 関連するPDBエントリー: 1WDL 1WDM
• 分子名称: Fatty oxidation complex alpha subunit, 3-ketoacyl-CoA thiolase, ZINC ION, ... (8 entities in total)
• 機能のキーワード: alpha2beta2 heterotetrameric complex, lyase, oxidoreductase-transferase complex, oxidoreductase/transferase
• 由来する生物種: Pseudomonas fragi; 詳細
• 細胞内の位置: Cytoplasm (By similarity): P28790
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 242324.54

構造登録者

Ishikawa, M.,Tsuchiya, D.,Oyama, T.,Tsunaka, Y.,Morikawa, K. (登録日: 2004-05-17, 公開日: 2004-07-27, 最終更新日: 2024-03-13)

主引用文献

Ishikawa, M.,Tsuchiya, D.,Oyama, T.,Tsunaka, Y.,Morikawa, K.
Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex
Embo J., 23:2745-2754, 2004

PubMed Abstract: The atomic view of the active site coupling termed channelling is a major subject in molecular biology. We have determined two distinct crystal structures of the bacterial multienzyme complex that catalyzes the last three sequential reactions in the fatty acid beta-oxidation cycle. The alpha2beta2 heterotetrameric structure shows the uneven ring architecture, where all the catalytic centers of 2-enoyl-CoA hydratase (ECH), L-3-hydroxyacyl-CoA dehydrogenase (HACD) and 3-ketoacyl-CoA thiolase (KACT) face a large inner solvent region. The substrate, anchored through the 3'-phosphate ADP moiety, allows the fatty acid tail to pivot from the ECH to HACD active sites, and finally to the KACT active site. Coupling with striking domain rearrangements, the incorporation of the tail into the KACT cavity and the relocation of 3'-phosphate ADP bring the reactive C2-C3 bond to the correct position for cleavage. The alpha-helical linker specific for the multienzyme contributes to the pivoting center formation and the substrate transfer through its deformation. This channelling mechanism could be applied to other beta-oxidation multienzymes, as revealed from the homology model of the human mitochondrial trifunctional enzyme complex.

PubMed: 15229654
DOI: 10.1038/sj.emboj.7600298

実験手法

X-RAY DIFFRACTION (2.5 Å)