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


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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.

Авторлар туралы

L. Dadinova

Shubnikov Institute of Crystallography; Moscow State University

Email: shtykova@ns.crys.ras.ru
Ресей, Leninskii pr. 59, Moscow, 119333; Moscow, 119992

E. Rodina

Moscow State University

Email: shtykova@ns.crys.ras.ru
Ресей, Moscow, 119992

N. Vorobyeva

Moscow State University

Email: shtykova@ns.crys.ras.ru
Ресей, Moscow, 119992

S. Kurilova

Moscow State University

Email: shtykova@ns.crys.ras.ru
Ресей, Moscow, 119992

T. Nazarova

Moscow State University

Email: shtykova@ns.crys.ras.ru
Ресей, Moscow, 119992

E. Shtykova

Shubnikov Institute of Crystallography; Moscow State University

Хат алмасуға жауапты Автор.
Email: shtykova@ns.crys.ras.ru
Ресей, Leninskii pr. 59, Moscow, 119333; Moscow, 119992

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