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

  • Structure of Macromolecular Compounds
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Abstract

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.

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Authors and Affiliations

  1. Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, Moscow, 119333, Russia

    L. A. Dadinova & E. V. Shtykova

  2. Moscow State University, Moscow, 119992, Russia

    L. A. Dadinova, E. V. Rodina, N. N. Vorobyeva, S. A. Kurilova, T. I. Nazarova & E. V. Shtykova

Authors
  1. L. A. Dadinova
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  2. E. V. Rodina
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  3. N. N. Vorobyeva
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  4. S. A. Kurilova
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  5. T. I. Nazarova
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  6. E. V. Shtykova
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Correspondence to E. V. Shtykova.

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Original Russian Text © L.A. Dadinova, E.V. Rodina, N.N. Vorobyeva, S.A. Kurilova, T.I. Nazarova, E.V. Shtykova, 2016, published in Kristallografiya, 2016, Vol. 61, No. 3, pp. 406–412.

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Dadinova, L.A., Rodina, E.V., Vorobyeva, N.N. et al. Structural investigations of E. Coli dihydrolipoamide dehydrogenase in solution: Small-angle X-ray scattering and molecular docking. Crystallogr. Rep. 61, 414–420 (2016). https://doi.org/10.1134/S1063774516030093

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  • DOI: https://doi.org/10.1134/S1063774516030093

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