Structure of the medium-chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution.
Structure of the medium-chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution.
复制标题
猪肝线粒体中链酰基辅酶 A 脱氢酶的结构（3A 分辨率）。
DOI：
10.1073/pnas.85.18.6677
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发表时间：
1988
影响因子：
11.1
通讯作者：
Wu,J
中科院分区：
文献类型：
--
作者：
Kim,JJ;Wu,J
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.
