Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 171, Issue 3, Pages 397-401Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2010.05.007
Keywords
Hore_18220; Fructokinase; FRY homolog; Fructose; ATP; Structure
Funding
- Academic Research Fund (ARF) [R154000245112]
- National University of Singapore (NUS)
- Polish Ministry of Science [188/N-DFG/2008/0]
- NIH [1R01 GM081680-01]
- Griffith University
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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 FRY, 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 beta-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. (C) 2010 Elsevier Inc. All rights reserved.
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