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首页> 外文期刊>Journal of Molecular Biology >SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXYGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELANDII
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SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXYGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELANDII

机译：双歧杆菌葡萄园2-羟基谷氨酸脱氢酶复合物脂酰域的溶液结构

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摘要

The three-dimensional solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii has been determined from nuclear magnetic resonance data by using distance geometry and dynamical simulated annealing refinement. The structure determination is based on a total of 580 experimentally derived distance constraints and 65 dihedral angle constraints. The solution structure is represented by an ensemble of 25 structures with an average root-mean-square deviation between the individual structures of the ensemble and the mean coordinates of 0.71 Angstrom for backbone atoms and 1.08 Angstrom for all heavy atoms. The overall fold of the lipoyl domain is that of a beta-barrel-sandwich hybrid. It consists of two almost parallel four-stranded anti-parallel beta-sheets formed around a well-defined hydrophobic core, with a central position of the single tryptophan 21. The lipoylation site, lysine 42, is found in a beta-turn at the far end of one of the sheets, and is close in space to a solvent-exposed loop comprising residues 7 to 15. The lipoyl domain displays a remarkable internal symmetry that projects one beta-sheet onto the other beta-sheet after rotation of approximately 180 degrees about a 2-fold rotational symmetry axis. There is close structural similarity between the structure of this 2-oxoglutarate dehydrogenase complex lipoyl domain and the structures of the lipoyl domains of pyruvate dehydrogenase complexes from Bacillus Stearothermophilus and Escherichia coli, and conformational differences occur primarily in a solvent-exposed loop close in space to the lipoylation site. The lipoyl domain structure is discussed in relation to the process of molecular recognition of lipoyl domains by their parent 2-oxo acid dehydrogenase. (C) 1996 Academic Press Limited. [References: 41]
机译：通过使用距离几何和动力学模拟退火精炼，从核磁共振数据中确定了来自葡萄固氮菌的2-氧戊二酸脱氢酶复合物的脂酰结构域的三维溶液结构。结构确定是基于总共580个实验得出的距离约束和65个二面角约束。溶液结构由25个结构的集合表示，该集合的单个结构之间的平均均方根偏差和骨架原子的平均坐标为0.71埃，所有重原子的平均坐标为1.08埃。脂酰结构域的整体折叠是β-桶-三明治混合体的折叠。它由围绕一个明确的疏水核形成的两个几乎平行的四链反平行β-折叠组成，具有单个色氨酸21的中心位置。脂酰化位点赖氨酸42位于β-转角处。一张纸的另一端，并在空间上靠近包含残基7至15的暴露于溶剂的环。脂酰结构域显示出显着的内部对称性，旋转约180度后，一个β纸会投影到另一张β纸上。围绕2倍旋转对称轴旋转1度。该2-氧代戊二酸脱氢酶复合物脂酰结构域的结构与嗜热脂肪芽孢杆菌和大肠杆菌的丙酮酸脱氢酶复合物的脂酰结构域的结构之间具有密切的结构相似性，并且构象差异主要发生在空间靠近空间的溶剂暴露环中。脂酰化位点。讨论了通过其母体2-氧代酸脱氢酶对脂酰结构域的分子识别过程的脂酰结构域结构。 （C）1996 Academic Press Limited。 [参考：41]

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