دورية أكاديمية
Structural and functional insights into the flexible β-hairpin of glycerol dehydrogenase.
| العنوان: | Structural and functional insights into the flexible β-hairpin of glycerol dehydrogenase. |
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| المؤلفون: | Park T; Department of Chemistry, Gwangju Institute of Science and Technology (GIST), Korea.; Steitz Center for Structural Biology, Gwangju Institute of Science and Technology (GIST), Korea., Hoang HN; Department of Molecular Medicine, Chonnam National University, Gwangju, Korea.; Hanoi Medical University, Hanoi, Vietnam., Kang JY; Steitz Center for Structural Biology, Gwangju Institute of Science and Technology (GIST), Korea.; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Korea., Park J; Steitz Center for Structural Biology, Gwangju Institute of Science and Technology (GIST), Korea.; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Korea., Mun SA; Steitz Center for Structural Biology, Gwangju Institute of Science and Technology (GIST), Korea.; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Korea., Jin M; Steitz Center for Structural Biology, Gwangju Institute of Science and Technology (GIST), Korea.; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Korea., Yang J; Steitz Center for Structural Biology, Gwangju Institute of Science and Technology (GIST), Korea.; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Korea., Jung CH; Department of Molecular Medicine, Chonnam National University, Gwangju, Korea.; Department of Chemistry, Chonnam National University, Gwangju, Korea., Eom SH; Department of Chemistry, Gwangju Institute of Science and Technology (GIST), Korea.; Steitz Center for Structural Biology, Gwangju Institute of Science and Technology (GIST), Korea.; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Korea. |
| المصدر: | The FEBS journal [FEBS J] 2023 Sep; Vol. 290 (17), pp. 4342-4355. Date of Electronic Publication: 2023 May 19. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 101229646 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1742-4658 (Electronic) Linking ISSN: 1742464X NLM ISO Abbreviation: FEBS J Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Oxford, UK : Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies, c2005- |
| مواضيع طبية MeSH: | NAD*/metabolism , Sugar Alcohol Dehydrogenases*/genetics , Sugar Alcohol Dehydrogenases*/chemistry , Sugar Alcohol Dehydrogenases*/metabolism, Glycerol/metabolism ; Oxidation-Reduction ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Kinetics ; Glutamate Dehydrogenase/metabolism |
| مستخلص: | During glycerol metabolism, the initial step of glycerol oxidation is catalysed by glycerol dehydrogenase (GDH), which converts glycerol to dihydroxyacetone in a NAD + -dependent manner via an ordered Bi-Bi kinetic mechanism. Structural studies conducted with GDH from various species have mainly elucidated structural details of the active site and ligand binding. However, the structure of the full GDH complex with both cofactor and substrate bound is not determined, and thus, the structural basis of the kinetic mechanism of GDH remains unclear. Here, we report the crystal structures of Escherichia coli GDH with a substrate analogue bound in the absence or presence of NAD + . Structural analyses including molecular dynamics simulations revealed that GDH possesses a flexible β-hairpin, and that during the ordered progression of the kinetic mechanism, the flexibility of the β-hairpin is reduced after NAD + binding. It was also observed that this alterable flexibility of the β-hairpin contributes to the cofactor binding and possibly to the catalytic efficiency of GDH. These findings suggest the importance of the flexible β-hairpin to GDH enzymatic activity and shed new light on the kinetic mechanism of GDH. (© 2023 Federation of European Biochemical Societies.) |
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| فهرسة مساهمة: | Keywords: crystal structure; glycerol dehydrogenase; kinetics; molecular dynamics simulation; ordered Bi-Bi mechanism |
| المشرفين على المادة: | EC 1.1.1.6 (glycerol dehydrogenase) 0U46U6E8UK (NAD) PDC6A3C0OX (Glycerol) EC 1.1.- (Sugar Alcohol Dehydrogenases) EC 1.4.1.2 (Glutamate Dehydrogenase) |
| تواريخ الأحداث: | Date Created: 20230511 Date Completed: 20230911 Latest Revision: 20230914 |
| رمز التحديث: | 20240829 |
| DOI: | 10.1111/febs.16813 |
| PMID: | 37165682 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1742-4658 |
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| DOI: | 10.1111/febs.16813 |