Structural investigations of E. Coli dihydrolipoamide dehydrogenase in solution: Small-angle X-ray scattering and molecular docking
- Авторы: Dadinova L.A.1,2, Rodina E.V.2, Vorobyeva N.N.2, Kurilova S.A.2, Nazarova T.I.2, Shtykova E.V.1,2
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Учреждения:
- Shubnikov Institute of Crystallography
- Moscow State University
- Выпуск: Том 61, № 3 (2016)
- Страницы: 414-420
- Раздел: Structure of Macromolecular Compounds
- URL: https://journals.rcsi.science/1063-7745/article/view/189997
- DOI: https://doi.org/10.1134/S1063774516030093
- ID: 189997
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Аннотация
Dihydrolipoamide dehydrogenase from Escherichia coli (LpD) is a bacterial enzyme that is involved in the central metabolism and shared in common between the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes. In the crystal structure, E. coli LpD is known to exist as a dimer. The present work is focused on analyzing the solution structure of LpD by small-angle X-ray scattering, molecular docking, and analytical ultracentrifugation. It was shown that in solution LpD exists as an equilibrium mixture of a dimer and a tetramer. The presence of oligomeric forms is determined by the multifunctionality of LpD in the cell, in particular, the required stoichiometry in the complexes.
Об авторах
L. Dadinova
Shubnikov Institute of Crystallography; Moscow State University
Email: shtykova@ns.crys.ras.ru
Россия, Leninskii pr. 59, Moscow, 119333; Moscow, 119992
E. Rodina
Moscow State University
Email: shtykova@ns.crys.ras.ru
Россия, Moscow, 119992
N. Vorobyeva
Moscow State University
Email: shtykova@ns.crys.ras.ru
Россия, Moscow, 119992
S. Kurilova
Moscow State University
Email: shtykova@ns.crys.ras.ru
Россия, Moscow, 119992
T. Nazarova
Moscow State University
Email: shtykova@ns.crys.ras.ru
Россия, Moscow, 119992
E. Shtykova
Shubnikov Institute of Crystallography; Moscow State University
Автор, ответственный за переписку.
Email: shtykova@ns.crys.ras.ru
Россия, Leninskii pr. 59, Moscow, 119333; Moscow, 119992
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