Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F
Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F
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DOI：
10.1038/22357
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发表时间：
1999-07-15
期刊：
影响因子：
64.8
通讯作者：
Cavanagh, J
中科院分区：
文献类型：
--
作者：
Feher, VA;Cavanagh, J
蛋白质主链和侧链表现出不同程度的灵活性，从而允许出现许多略有不同但相关的构象亚状态(1)。已知这种波动在时间尺度和幅度上都有所不同，从甲基的旋转（纳秒）到埋藏酪氨酸环的翻转（秒）(2,3)。由于蛋白质功能的许多机制需要构象变化，因此有人提出，其中一些基态波动与蛋白质功能有关(4)。但到底运动的哪些方面在功能上相关仍有待确定。到目前为止，只有几个例子可以将函数与已知幅度和时间尺度的结构波动相关联(5,6)。作为枯草芽孢杆菌反应调节剂 Spo0F 作用机制研究的一部分，我们探索了运动特征与蛋白质-蛋白质相互作用之间的关系。在这里，我们使用一组核磁共振 N-15 弛豫测量来确定 Spo0F 主链波动在皮秒到毫秒时间尺度上的相对时间尺度。我们表明，在毫秒时间尺度上运动的区域与已知对蛋白质-蛋白质相互作用至关重要的残基和表面相关。
Protein backbones and side chains display varying degrees of flexibility, which allows many slightly different but related conformational substates to occur(1). Such fluctuations are known to differ in both timescale and magnitude, from rotation of methyl groups (nanoseconds) to the flipping of buried tyrosine rings (seconds)(2,3), Because many mechanisms for protein function require conformational change, it has been proposed that some of these ground-state fluctuations are related to protein function(4). But exactly which aspects of motion are functionally relevant remains to be determined. Only a few examples so far exist where function can be correlated to structural fluctuations with known magnitude and timescale(5,6). As part of an investigation of the mechanism of action of the Bacillus subtilis response regulator Spo0F, we have explored the relationship between the motional characteristics and protein-protein interactions. Here we use a set of nuclear magnetic resonance N-15 relaxation measurements to determine the relative timescales of Spo0F backbone fluctuations on the picosecond-to-millisecond timescale, We show that regions having motion on the millisecond timescale correlate with residues and surfaces that are known to be critical for protein-protein interactions.