Crystal structure of a fructokinase homolog from Halothermothrix orenii

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Chua, Teck Khiang
Seetharaman, J
Kasprzak, Joanna M
Ng, Cherlyn
Patel, Bharat KC
Love, Christopher
Bujnicki, Janusz M
Sivaraman, J
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2010
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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 ߭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.

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Journal of Structural Biology

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171

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3

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Biochemistry and cell biology

Biochemistry and cell biology not elsewhere classified

Zoology

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