Crystal structure of human mitochondrial trifunctional protein, a fatty acid β-oxidation metabolon.

ABSTRACT: Membrane-bound mitochondrial trifunctional protein (TFP) catalyzes β-oxidation of long chain fatty acyl-CoAs, employing 2-enoyl-CoA hydratase (ECH), 3-hydroxyl-CoA dehydrogenase (HAD), and 3-ketothiolase (KT) activities consecutively. Inherited deficiency of TFP is a recessive genetic disease, manifesting in hypoketotic hypoglycemia, cardiomyopathy, and sudden death. We have determined the crystal structure of human TFP at 3.6-Å resolution. The biological unit of the protein is α₂β₂ The overall structure of the heterotetramer is the same as that observed by cryo-EM methods. The two β-subunits make a tightly bound homodimer at the center, and two α-subunits are bound to each side of the β₂ dimer, creating an arc, which binds on its concave side to the mitoch

SUBMITTER: Xia C 

PROVIDER: S-EPMC6442613 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature