Direct observation of correlated interdomain motion in alcohol dehydrogenase
Direct observation of correlated interdomain motion in alcohol dehydrogenase
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DOI：
10.1103/physrevlett.101.138102
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发表时间：
2008-09-26
影响因子：
8.6
通讯作者：
Richter, Dieter
中科院分区：
文献类型：
--
作者：
Biehl, Ralf;Hoffmann, Bernd;Richter, Dieter
蛋白质结构域间运动对于激活或促进生化功能至关重要。采用中子旋回光谱法直接观察了蛋白醇脱氢酶的结构域动力学。结构域的集体运动与结合和催化结构域之间的间隙打开动力学有关，从而使功能重要辅因子的结合和释放成为可能。由于辅因子的结合导致结构域复合物的整体硬化，导致裂缝打开模式硬化。
Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spinecho spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.