1itw
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the monomeric isocitrate dehydrogenase in complex with isocitrate and Mn
OverviewOverview
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 CO(2) 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 A 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.
About this StructureAbout this Structure
1ITW is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the monomeric isocitrate dehydrogenase: evidence of a protein monomerization by a domain duplication., Yasutake Y, Watanabe S, Yao M, Takada Y, Fukunaga N, Tanaka I, Structure. 2002 Dec;10(12):1637-48. PMID:12467571
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