STRUCTURE OF A BACTERIAL ENZYME REGULATED BY PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE
STRUCTURE OF A BACTERIAL ENZYME REGULATED BY PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE
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DOI：
10.1073/pnas.86.22.8635
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发表时间：
1989-11-01
影响因子：
11.1
通讯作者：
STROUD, RM
中科院分区：
文献类型：
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作者：
HURLEY, JH;THORSNESS, PE;STROUD, RM
来自大肠杆菌的异柠檬酸脱氢酶[theo-DS-isocitrate：NADP+氧化还原酶（脱羧），EC www.example.com]的结构已被解析并在2.5埃下精制。分辨率和拓扑结构不同于任何其他脱氢酶。这种酶，一个相同的416个残基亚基的二聚体，通过在Ser-113磷酸化而失活，Ser-113位于一个域间口袋的边缘，该口袋也包含许多在异柠檬酸脱氢酶和异丙基苹果酸脱氢酶之间保守的残基。异柠檬酸脱氢酶含有一个不寻常的clasp样结构域，其中二聚体中的两条多肽链互锁。基于异柠檬酸脱氢酶的结构和与异丙基苹果酸脱氢酶的保守性，我们认为活性位点位于靠近磷酸化位点的域间口袋中。
The structure of isocitrate dehydrogenase [theo-DS-isocitrate:NADP+ oxidoreductase (decarboxylating), EC 1.1.1.42] from Escherichia coli has been solved and refined at 2.5 .ANG. resolution and is topologically different from that of any other dehydrogenase. This enzyme, a dimer of identical 416-residue subunits, is inactivated by phosphorylation at Ser-113, which lies at the edge of an interdomain pocket that also contains many residues conserved between isocitrate dehydrogenase and isopropylmalate dehydrogenase. Isocitrate dehydrogenase contains an unusual clasp-like domain in which both polypeptide chains in the dimer interlock. Based on the structure of isocitrate dehydrogenase and conservation with isopropylmalate dehydrogenase, we suggest that the active site lies in an interdomain pocket close to the phosphorylation site.