3HLK
Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)
Summary for 3HLK
| Entry DOI | 10.2210/pdb3hlk/pdb |
| Descriptor | Acyl-coenzyme A thioesterase 2, mitochondrial (2 entities in total) |
| Functional Keywords | alpha/beta hydrolase, alternative splicing, hydrolase, mitochondrion, polymorphism, serine esterase, transit peptide |
| Biological source | Homo sapiens (human) |
| Cellular location | Mitochondrion : P49753 |
| Total number of polymer chains | 2 |
| Total formula weight | 99355.49 |
| Authors | Mandel, C.R.,Tweel, B.,Tong, L. (deposition date: 2009-05-27, release date: 2009-06-23, Last modification date: 2024-11-06) |
| Primary citation | Mandel, C.R.,Tweel, B.,Tong, L. Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2) Biochem.Biophys.Res.Commun., 385:630-633, 2009 Cited by 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: 19497300DOI: 10.1016/j.bbrc.2009.05.122 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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