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

作者信息

Karlström Mikael, Steen Ida Helene, Tibbelin Gudrun, Lien Torleiv, Birkeland Nils-Kåre, Ladenstein Rudolf

机构信息

Karolinska Institutet, NOVUM, Center for Structural Biochemistry, S-14157 Huddinge, Sweden.

出版信息

Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2162-4. doi: 10.1107/s0907444902016050. Epub 2002 Nov 23.

DOI:10.1107/s0907444902016050
PMID:12454487
Abstract

Isocitrate dehydrogenase (IDH) catalyses the dehydrogenation and decarboxylation of isocitrate to alpha-ketoglutarate and CO(2) 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 A with synchrotron radiation and belong to space group P4(3)2(1)2. 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 A with Cu Kalpha radiation and belong to space group P2(1)2(1)2(1). The structures will be helpful in the study of the factors responsible for thermostability and the evolutionary relationships of IDHs.

摘要

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