Crystallization and preliminary X-ray structure analysis of isocitrate dehydrogenase from two hyperthermophiles, Aeropyrum pernix and Thermotoga maritima

Isocitrate dehydrogenase (IDH) catalyses the dehydrogenation and decarboxylation of isocitrate to α‐ketoglutarate and CO2 with NAD or NADP as cofactor. IDH from Aeropyrum pernix is the most thermostable IDH identified. Crystals of A. pernix IDH diffracted to 2.6 Å with synchrotron radiation and belo...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-12, Vol.58 (12), p.2162-2164
Main Authors: Karlström, Mikael, Steen, Ida Helene, Tibbelin, Gudrun, Lien, Torleiv, Birkeland, Nils-Kåre, Ladenstein, Rudolf
Format: Article
Language:English
Subjects:
Crystallization
Crystallography, X-Ray
Desulfurococcaceae - enzymology
isocitrate dehydrogenase
Isocitrate Dehydrogenase - chemistry
Protein Conformation
thermostability
Thermotoga maritima - enzymology
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Summary:Isocitrate dehydrogenase (IDH) catalyses the dehydrogenation and decarboxylation of isocitrate to α‐ketoglutarate and CO2 with NAD or NADP as cofactor. IDH from Aeropyrum pernix is the most thermostable IDH identified. Crystals of A. pernix IDH diffracted to 2.6 Å with synchrotron radiation and belong to space group P43212. IDH from Thermotoga maritima is the only IDH that has been characterized as homotetrameric and might be an evolutionary link between two different IDH subfamilies. T. maritima IDH crystals diffracted to 2.8 Å with Cu Kα radiation and belong to space group P212121. The structures will be helpful in the study of the factors responsible for thermostability and the evolutionary relationships of IDHs.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444902016050