Structural investigations of E. Coli dihydrolipoamide dehydrogenase in solution: Small-angle X-ray scattering and molecular docking
- Авторлар: 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
-
Мекемелер:
- Shubnikov Institute of Crystallography
- Moscow State University
- Шығарылым: Том 61, № 3 (2016)
- Беттер: 414-420
- Бөлім: Structure of Macromolecular Compounds
- URL: https://journals.rcsi.science/1063-7745/article/view/189997
- DOI: https://doi.org/10.1134/S1063774516030093
- ID: 189997
Дәйексөз келтіру
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
Қосымша файлдар
