2D3T

Fatty Acid beta-oxidation multienzyme complex from Pseudomonas Fragi, Form V

2D3T の概要

• エントリーDOI: 10.2210/pdb2d3t/pdb
• 関連するPDBエントリー: 1WDK 1WDL 1WDM
• 分子名称: Fatty oxidation complex alpha subunit, 3-ketoacyl-CoA thiolase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 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: 240455.98

構造登録者

Tsuchiya, D.,Shimizu, N.,Ishikawa, M.,Suzuki, Y.,Morikawa, K. (登録日: 2005-10-01, 公開日: 2006-02-21, 最終更新日: 2023-10-25)

主引用文献

Tsuchiya, D.,Shimizu, N.,Ishikawa, M.,Suzuki, Y.,Morikawa, K.
Ligand-Induced Domain Rearrangement of Fatty Acid beta-Oxidation Multienzyme Complex
Structure, 14:237-246, 2006

PubMed Abstract: The quaternary structure of a fatty acid beta-oxidation multienzyme complex, catalyzing three sequential reactions, was investigated by X-ray crystallographic and small-angle X-ray solution scattering analyses. X-ray crystallography revealed an intermediate structure of the complex among the previously reported structures. However, the theoretical scattering curves calculated from the crystal structures remarkably disagree with the experimental profiles. Instead, an ensemble of the atomic models, which were all calculated by rigid-body optimization, reasonably explained the experimental data. These structures significantly differ from those in the crystals, but they maintain the substrate binding pocket at the domain boundary. Comparisons among these structures indicated that binding of 3-hydroxyhexadecanoyl-CoA or nicotinamide adenine dinucleotide induces domain rearrangements in the complex. The conformational changes suggest the structural events occurring during the chain reaction catalyzed by the multienzyme complex.

PubMed: 16472743
DOI: 10.1016/j.str.2005.10.011

実験手法

X-RAY DIFFRACTION (3.4 Å)