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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 58; no. 12; pp. 2162 - 2164
• Main Authors: Karlström, Mikael, Steen, Ida Helene, Tibbelin, Gudrun, Lien, Torleiv, Birkeland, Nils-Kåre, Ladenstein, Rudolf
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01-12-2002
• Subjects: Crystallization; Crystallography, X-Ray; Desulfurococcaceae - enzymology; isocitrate dehydrogenase; Isocitrate Dehydrogenase - chemistry; Medicin och hälsovetenskap; Protein Conformation; thermostability; Thermotoga maritima - enzymology
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444902016050

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.