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首页> 外文期刊>Crystallography reports >Structural investigations of E-Coli dihydrolipoamide dehydrogenase in solution: Small-angle X-ray scattering and molecular docking
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Structural investigations of E-Coli dihydrolipoamide dehydrogenase in solution: Small-angle X-ray scattering and molecular docking

机译:溶液中E-Coli二氢脂酰胺脱氢酶的结构研究:小角度X射线散射和分子对接

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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.
机译:来自大肠杆菌(LpD)的二氢脂酰胺脱氢酶是一种细菌酶,参与中央代谢,并且在丙酮酸脱氢酶和2-氧戊二酸脱氢酶复合物之间共享。在晶体结构中,已知大肠杆菌LpD以二聚体形式存在。目前的工作集中在通过小角度X射线散射,分子对接和分析超离心来分析LpD的溶液结构。结果表明,LpD在溶液中以二聚物和四聚物的平衡混合物形式存在。寡聚形式的存在取决于细胞中LpD的多功能性,特别是复合物中所需的化学计量。

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