1F14

L-3-HYDROXYACYL-COA DEHYDROGENASE (APO)

1F14 の概要

• エントリーDOI: 10.2210/pdb1f14/pdb
• 関連するPDBエントリー: 1F0Y 1F12 1F17 3HAD
• 分子名称: L-3-HYDROXYACYL-COA DEHYDROGENASE (2 entities in total)
• 機能のキーワード: l-3-hydroxyacyl-coa (apoenzyme), oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion matrix: Q16836
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67791.65

構造登録者

Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.,Banaszak, L.J. (登録日: 2000-05-18, 公開日: 2000-09-27, 最終更新日: 2024-02-07)

主引用文献

Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.,Banaszak, L.J.
Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase.
J.Biol.Chem., 275:27186-27196, 2000

PubMed Abstract: l-3-Hydroxyacyl-CoA dehydrogenase reversibly catalyzes the conversion of l-3-hydroxyacyl-CoA to 3-ketoacyl-CoA concomitant with the reduction of NAD(+) to NADH as part of the beta-oxidation spiral. In this report, crystal structures have been solved for the apoenzyme, binary complexes of the enzyme with reduced cofactor or 3-hydroxybutyryl-CoA substrate, and an abortive ternary complex of the enzyme with NAD(+) and acetoacetyl-CoA. The models illustrate positioning of cofactor and substrate within the active site of the enzyme. Comparison of these structures with the previous model of the enzyme-NAD(+) complex reveals that although significant shifting of the NAD(+)-binding domain relative to the C-terminal domain occurs in the ternary and substrate-bound complexes, there are few differences between the apoenzyme and cofactor-bound complexes. Analysis of these models clarifies the role of key amino acids implicated in catalysis and highlights additional critical residues. Furthermore, a novel charge transfer complex has been identified in the course of abortive ternary complex formation, and its characterization provides additional insight into aspects of the catalytic mechanism of l-3-hydroxyacyl-CoA dehydrogenase.

PubMed: 10840044

実験手法

X-RAY DIFFRACTION (2.3 Å)