Structure of the monomeric isocitrate dehydrogenase: Evidence of a protein momomerization by a domain duplication

被引：49

作者：

Yasutake, Y ^{[1
]}

Watanabe, S ^{[1
]}

Yao, M ^{[1
]}

Takada, Y ^{[1
]}

Fukunaga, N ^{[1
]}

Tanaka, I ^{[1
]}

机构：

[1] Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Kita Ku, Sapporo, Hokkaido 0600810, Japan

来源：

STRUCTURE | 2002年 / 10卷 / 12期

关键词：

crystal structure; gene duplication; 3D domain swapping; monomeric IDH; molecular evolution; beta-decarboxylating dehydrogenase family;

D O I：

10.1016/S0969-2126(02)00904-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

NADP(+)-dependent isocitrate dehydrogenase is a member of the beta-decarboxylating dehydrogenase family and catalyzes the oxidative decarboxylation reaction from 2R,3S-isocitrate to yield 2-oxoglutarate and CO2 in the Krebs cycle. Although most prokaryotic NADP(+)-dependent isocitrate dehydrogenases (IDHs) are homodimeric enzymes, the monomeric IDH with a molecular weight of 80-100 kDa has been found in a few species of bacteria. The 1.95 Angstrom crystal structure of the monomeric IDH revealed that it consists of two distinct domains, and its folding topology is related to the dimeric IDH. The structure of the large domain repeats a motif observed in the dimeric IDH. Such a fusional structure by domain duplication enables a single polypeptide chain to form a structure at the catalytic site that is homologous to the dimeric IDH, the catalytic site of which is located at the interface of two identical subunits.

引用

页码：1637 / 1648

页数：12

共 43 条

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