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

Journal Article · · Biochem. Biophys. Res. Commun.
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 2.1 {angstrom} 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.
Research Organization:
Argonne National Laboratory (ANL)
Sponsoring Organization:
USDOE
OSTI ID:
1005774
Journal Information:
Biochem. Biophys. Res. Commun., Journal Name: Biochem. Biophys. Res. Commun. Journal Issue: (4) ; 08, 2009 Vol. 385; ISSN 0006-291X; ISSN BBRCA9
Country of Publication:
United States
Language:
ENGLISH

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