RIGID PROTEIN MOTION AS A MODEL FOR CRYSTALLOGRAPHIC TEMPERATURE FACTORS
RIGID PROTEIN MOTION AS A MODEL FOR CRYSTALLOGRAPHIC TEMPERATURE FACTORS
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DOI：
10.1073/pnas.88.7.2773
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发表时间：
1991-04-01
影响因子：
11.1
通讯作者：
WEIS, WI
中科院分区：
文献类型：
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作者：
KURIYAN, J;WEIS, WI
刚性分子的振动在多大程度上可以模拟蛋白质的晶体学温度因子分布已被检查。 对于考虑的所有蛋白质，包括流感病毒血凝素、谷胱甘肽还原酶、肌红蛋白、肌红蛋白和链霉亲和素，简单的10参数模型[V. Schomaker和K. N. 03 The Dog（1968） B 24，63-76]被发现在各向同性的骨干均方位移的最大值和最小值的图案的定性重现。 刚性分子和单个原子温度因子之间的大偏差被发现与血凝素中的一个区域相关，该区域的精细结构模型是不满意的，并且在部分不正确的myohemerythrin模型中的结构中存在错误。 对于高分辨率的谷胱甘肽还原酶结构，更好的结果是获得治疗的结构中的每个紧凑的域作为独立的刚体。 该方法允许可靠的温度因素的改进，引入最小的参数，并可能证明有用的模型在早期阶段的X射线结构细化的评估。 虽然这些结果本身并没有建立潜在的位移的性质，刚性蛋白质模型在再现温度因子分布的定性特征方面的成功表明，在任何晶体学热参数的解释中，都应考虑刚体细化结果。
The extent to which the librations of rigid molecules can model the crystallographic temperature factor profiles of proteins has been examined. For all proteins considered, including influenza virus hemagglutinin, glutathione reductase, myohemerythrin, myoglobin, and streptavidin, a simple 10-parameter model [V. Schomaker and K. N. Trueblood (1968) Acta Crystallogr. Sect. B 24, 63-76] is found to reproduce qualitatively the patterns of maxima and minima in the isotropic backbone mean-square displacements. Large deviations between the rigid molecule and individual atomic temperature factors are found to be correlated with a region in hemagglutinin for which the refined structural model is unsatisfactory and with errors in the structure in a partially incorrect model of myohemerythrin. For the high-resolution glutathione reductase structure, better results are obtained on treating each of the compact domains in the structure as independent rigid bodies. The method allows for the refinement of reliable temperature factors with the introduction of minimal parameters and may prove useful for the evaluation of models in the early stages of x-ray structure refinement. While these results by themselves do not establish the nature of the underlying displacements, the success of the rigid protein model in reproducing qualitative features of temperature factor profiles suggests that rigid body refinement results should be considered in any interpretation of crystallographic thermal parameters.