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|Title:||Crystal structure of a fructokinase homolog from Halothermothrix orenii||Authors:||Chua, T.K.
|Issue Date:||Sep-2010||Citation:||Chua, T.K., Seetharaman, J., Kasprzak, J.M., Ng, C., Patel, B.K.C., Love, C., Bujnicki, J.M., Sivaraman, J. (2010-09). Crystal structure of a fructokinase homolog from Halothermothrix orenii. Journal of Structural Biology 171 (3) : 397-401. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jsb.2010.05.007||Abstract:||Fructokinase (FRK; EC 184.108.40.206) catalyzes the phosphorylation of d-fructose to d-fructose 6-phosphate (F6P). This irreversible and near rate-limiting step is a central and regulatory process in plants and bacteria, which channels fructose into a metabolically active state for glycolysis. Towards understanding the mechanism of FRK, here we report the crystal structure of a FRK homolog from a thermohalophilic bacterium Halothermothrix orenii (Hore_18220 in sequence databases). The structure of the Hore_18220 protein reveals a catalytic domain with a Rossmann-like fold and a β-sheet " lid" for dimerization. Based on comparison of Hore_18220 to structures of related proteins, we propose its mechanism of action, in which the lid serves to regulate access to the substrate binding sites. Close relationship of Hore_18220 and plant FRK enzymes allows us to propose a model for the structure and function of FRKs. © 2010 Elsevier Inc.||Source Title:||Journal of Structural Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/67629||ISSN:||10478477||DOI:||10.1016/j.jsb.2010.05.007|
|Appears in Collections:||Staff Publications|
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