کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5914914 | 1162762 | 2010 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Crystal structure of a fructokinase homolog from Halothermothrix orenii
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Crystal structure of a fructokinase homolog from Halothermothrix orenii Crystal structure of a fructokinase homolog from Halothermothrix orenii](/preview/png/5914914.png)
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 171, Issue 3, September 2010, Pages 397-401
Journal: Journal of Structural Biology - Volume 171, Issue 3, September 2010, Pages 397-401
نویسندگان
Teck Khiang Chua, J. Seetharaman, Joanna M. Kasprzak, Cherlyn Ng, Bharat K.C. Patel, Christopher Love, Janusz M. Bujnicki, J. Sivaraman,