Structure of the medium-chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution.
The three-dimensional structure of the medium-chain acyl-CoA dehydrogenase (EC 1.3.99.3) from pig liver mitochondria has been determined to 3.0-A resolution by the x-ray diffraction method. The enzyme is a tetramer of four identical 43-kDa subunits and contains one equivalent of flavin adenine dinucleotide (FAD) per subunit. The polypeptide is folded into three domains. The N-terminal and the C-terminal domains are composed mainly of alpha-helices, and the middle domain is packed with orthogonal beta-sheets. The FAD has an extended conformation: the flavin ring lies between the N-terminal and the beta-sheet domains, and the adenine moiety is found at the junction between the C-terminal and the beta-sheet domains of one subunit and the C-terminal domain of a neighboring subunit. The polypeptide chain folding near the FAD binding site is different from those observed in other flavoproteins, such as glutathione reductase and glycolate oxidase.
Kim
J J
JJ
Department of Biochemistry, Medical College of Wisconsin, Milwaukee 53226.
Wu
J
J
D044944:Acyl-CoA Dehydrogenases / Q000032:analysis*; D000818:Animals; D003461:Crystallography; D005182:Flavin-Adenine Dinucleotide; D008930:Mitochondria, Liver / Q000201:enzymology*; D008958:Models, Molecular; D011487:Protein Conformation; D013552:Swine; D014961:X-Ray Diffraction
D005182:Flavin-Adenine Dinucleotide; D044944:Acyl-CoA Dehydrogenases