Mandel_2009_Biochem.Biophys.Res.Commun_385_630

Reference

Title : Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2) - Mandel_2009_Biochem.Biophys.Res.Commun_385_630
Author(s) : Mandel CR , Tweel B , Tong L
Ref : Biochemical & Biophysical Research Communications , 385 :630 , 2009
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.

PubMedSearch : Mandel_2009_Biochem.Biophys.Res.Commun_385_630
PubMedID: 19497300
Gene_locus related to this paper: human-ACOT2

Related information

Gene_locus human-ACOT2
Family human-ACOT2    Acyl-CoA_Thioesterase
Structure human-ACOT2    Acyl-CoA_Thioesterase    3HLK

Citations formats

Mandel CR, Tweel B, Tong L (2009)
Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)
Biochemical & Biophysical Research Communications 385 :630

Mandel CR, Tweel B, Tong L (2009)
Biochemical & Biophysical Research Communications 385 :630