Structural investigations of E. Coli dihydrolipoamide dehydrogenase in solution: Small-angle X-ray scattering and molecular docking
- 作者: 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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隶属关系:
- Shubnikov Institute of Crystallography
- Moscow State University
- 期: 卷 61, 编号 3 (2016)
- 页面: 414-420
- 栏目: 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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详细
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.
作者简介
L. Dadinova
Shubnikov Institute of Crystallography; Moscow State University
Email: shtykova@ns.crys.ras.ru
俄罗斯联邦, Leninskii pr. 59, Moscow, 119333; Moscow, 119992
E. Rodina
Moscow State University
Email: shtykova@ns.crys.ras.ru
俄罗斯联邦, Moscow, 119992
N. Vorobyeva
Moscow State University
Email: shtykova@ns.crys.ras.ru
俄罗斯联邦, Moscow, 119992
S. Kurilova
Moscow State University
Email: shtykova@ns.crys.ras.ru
俄罗斯联邦, Moscow, 119992
T. Nazarova
Moscow State University
Email: shtykova@ns.crys.ras.ru
俄罗斯联邦, Moscow, 119992
E. Shtykova
Shubnikov Institute of Crystallography; Moscow State University
编辑信件的主要联系方式.
Email: shtykova@ns.crys.ras.ru
俄罗斯联邦, Leninskii pr. 59, Moscow, 119333; Moscow, 119992
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