structural investigations of e coli dihydrolipoamide dehydrogenase in solution small angle x ray scattering and molecular docking

Autor:	L. A. Dadinova, E. V. Rodina, N. N. Vorobyeva, S. A. Kurilova, T. I. Nazarova, E. V. Shtykova
Rok vydání:	2016
Předmět:	Docking (molecular) Chemistry Dimer Crystallography Pyruvate dehydrogenase complex hemic and lymphatic diseases Dehydrogenase Small-angle X-ray scattering Escherichia coli Dihydrolipoamide dehydrogenase Tetramer
Zdroj:	Microsoft Academic Graph
ISSN:	1562-689X 1063-7745
DOI:	10.1134/S1063774516030093/fulltext.html
Popis:	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.
Databáze:	OpenAIRE
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