3HLK

Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)

3HLK の概要

• エントリーDOI: 10.2210/pdb3hlk/pdb
• 分子名称: Acyl-coenzyme A thioesterase 2, mitochondrial (2 entities in total)
• 機能のキーワード: alpha/beta hydrolase, alternative splicing, hydrolase, mitochondrion, polymorphism, serine esterase, transit peptide
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion : P49753
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99355.49

構造登録者

Mandel, C.R.,Tweel, B.,Tong, L. (登録日: 2009-05-27, 公開日: 2009-06-23, 最終更新日: 2024-11-06)

主引用文献

Mandel, C.R.,Tweel, B.,Tong, L.
Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)
Biochem.Biophys.Res.Commun., 385:630-633, 2009

PubMed Abstract: Acyl-CoA thioesterases (ACOTs) catalyze the hydrolysis of CoA esters to free CoA and carboxylic acids and have important functions in lipid metabolism and other cellular processes. Type I ACOTs are found only in animals and contain an alpha/beta hydrolase domain, through currently no structural information is available on any of these enzymes. We report here the crystal structure at 2.1A resolution of human mitochondrial ACOT2, a type I enzyme. The structure contains two domains, N and C domains. The C domain has the alpha/beta hydrolase fold, with the catalytic triad Ser294-His422-Asp388. The N domain contains a seven-stranded beta-sandwich, which has some distant structural homologs in other proteins. The active site is located in a large pocket at the interface between the two domains. The structural information has significant relevance for other type I ACOTs and related enzymes.

PubMed: 19497300
DOI: 10.1016/j.bbrc.2009.05.122

実験手法

X-RAY DIFFRACTION (2.1 Å)