Structural investigations of E. Coli dihydrolipoamide dehydrogenase in solution: Small-angle X-ray scattering and molecular docking


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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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