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首页> 外文期刊>Journal of Molecular Biology >Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy
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Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy

机译：溶液NMR光谱研究配体诱导的麦芽糖糊精结合蛋白的结构变化

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摘要

Solution NMR studies on the physiologically relevant ligand-free and maltotriose-bound states of maltodextrin-binding protein (MBP) are presented. Together with existing data on MBP in complex with beta -cyclodextrin (non-physiological, inactive ligand), these new results provide valuable information on changes in local structure, dynamics and global fold that occur upon Ligand binding to this two-domain protein. By measuring a large number of different one-bond residual dipolar couplings, the domain conformations, critical for biological function, were investigated for all three states of MBP. Structural models of the solution conformation of MBP in a number of different forms were generated from the experimental dipolar coupling data and X-ray crystal structures using a quasi-rigid-body domain orientation algorithm implemented in the structure calculation program CNS. Excellent agreement between relative domain orientations in Ligand-free and maltotriose-bound solution conformations and the corresponding crystal structures is observed. These results are in contrast to those obtained for the MBP/beta -cyclodextrin complex where the solution state is found to be similar to 10 degrees more closed than the crystalline state. The present study highlights the utility of residual dipolar couplings for orienting protein domains or macromolecules with respect to each other. (C) 2001 Academic Press. [References: 74]
机译：提出了对与麦芽糖糊精结合蛋白（MBP）生理相关的无配体和麦芽三糖结合状态的溶液NMR研究。这些新结果连同与β-环糊精（非生理性，非活性配体）复合的MBP的现有数据一起，提供了有关配体结合至此两个域蛋白后发生的局部结构，动力学和全局折叠变化的有价值的信息。通过测量大量不同的单键残留偶极偶合，研究了对于MBP的所有三个状态而言对生物学功能至关重要的结构域构象。使用结构计算程序CNS中实现的准刚体域取向算法，通过实验偶极耦合数据和X射线晶体结构，生成了多种形式的MBP溶液构象的结构模型。观察到无配体和麦芽三糖结合的溶液构象中的相对域取向与相应的晶体结构之间的极好的一致性。这些结果与从MBP /β-环糊精复合物获得的结果相反，在MBP /β-环糊精络合物中发现溶液状态比结晶状态封闭度接近10度。本研究强调了残留的偶极偶合对于定向蛋白质结构域或大分子彼此的实用性。 （C）2001学术出版社。 [参考：74]

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