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Preliminary crystallographic studies of an extremely thermostable KDG aldolase from Sulfolobus solfataricus


Reference:

Hendry, E. J., Buchanan, C. L., Russell, R. J. M., Hough, D. W., Reeve, C. D., Danson, M. J. and Taylor, G. L., 2000. Preliminary crystallographic studies of an extremely thermostable KDG aldolase from Sulfolobus solfataricus. Acta Crystallographica Section D-Biological Crystallography, 56, pp. 1437-1439.

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Abstract

Crystals have been grown of 2-keto-3-deoxygluconate aldolase (KDG aldolase) from the hyperthermophilic archaeon Sulfolobus solfataricus that diffract to 2.2 Angstrom resolution. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. S. solfataricus grows optimally at 353 K and the enzyme itself has a half-life of 2.5 h at 373 K. Knowledge of the crystal structure of KDG aldolase will further understanding of the basis of protein hyperthermostability and create a target for site-directed mutagenesis of active-site residues, with the aim of altering substrate specificity. Three crystal forms have been obtained: orthorhombic crystals of space group P2(1)2(1)2(1), which diffract to beyond 2.15 Angstrom, monoclinic crystals of space group C2, which diffract to 2.2 Angstrom, and cubic crystals of space group P4(2)32, which diffract to 3.4 Angstrom.

Details

Item Type Articles
CreatorsHendry, E. J., Buchanan, C. L., Russell, R. J. M., Hough, D. W., Reeve, C. D., Danson, M. J. and Taylor, G. L.
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code4436
Additional InformationID number: ISI:000165336100013

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