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 Halothermothrixorenii (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.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Chua TK,Seetharaman J,Kasprzak JM,Ng C,Patel BK,Love C,Bujnicki JM,Sivaraman Jdoi
10.1016/j.jsb.2010.05.007subject
Has Abstractpub_date
2010-09-01 00:00:00pages
397-401issue
3eissn
1047-8477issn
1095-8657pii
S1047-8477(10)00149-8journal_volume
171pub_type
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journal_title：Journal of structural biology
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doi：10.1006/jsbi.1998.4000
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