2iv0

File:2iv0.gif

spinqualitylabelsall models 2iv0, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS

OverviewOverview

Isocitrate dehydrogenase from Archaeoglobus fulgidus (AfIDH) has an, apparent melting temperature (T (m)) of 98.5 degrees C. To identify the, structural features involved in thermal stabilization of AfIDH, the, structure was solved to 2.5 A resolution. AfIDH was strikingly similar to, mesophilic IDH from Escherichia coli (EcIDH) and displayed almost the same, number of ion pairs and ionic networks. However, two unique inter-domain, networks were present in AfIDH; one three-membered ionic network between, the large and the small domain and one four-membered ionic network between, the clasp and the small domain. The latter ionic network was presumably, reduced in size when the clasp domain of AfIDH was swapped with that of, EcIDH and the T (m) decreased by 18 degrees C. Contrarily, EcIDH ... [(full description)]

About this StructureAbout this Structure

2IV0 is a [Single protein] structure of sequence from [Archaeoglobus fulgidus] with ZN and CL as [ligands]. Active as [Isocitrate dehydrogenase (NADP(+))], with EC number [1.1.1.42]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers., Stokke R, Karlstrom M, Yang N, Leiros I, Ladenstein R, Birkeland NK, Steen IH, Extremophiles. 2007 May;11(3):481-93. Epub 2007 Mar 31. PMID:17401542

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