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. 1988 Sep;85(18):6677–6681. doi: 10.1073/pnas.85.18.6677

Structure of the medium-chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution.

J J Kim 1, J Wu 1
PMCID: PMC282040  PMID: 3413116

Abstract

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.

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Selected References

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