Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jsb.2010.05.007
Title: Crystal structure of a fructokinase homolog from Halothermothrix orenii
Authors: Chua, T.K. 
Seetharaman, J.
Kasprzak, J.M.
Ng, C.
Patel, B.K.C.
Love, C.
Bujnicki, J.M.
Sivaraman, J. 
Keywords: ATP
FRK homolog
Fructokinase
Fructose
Hore_18220
Structure
Issue Date: Sep-2010
Source: 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 2.7.1.4) 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
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