大肠杆菌素E3与免疫蛋白3的缔合和解离动力学：理论与实验的趋同
Association and dissociation kinetics of colicin E3 and immunity protein 3: convergence of theory and experiment.
作者信息
Zhou Huan-Xiang
机构信息
Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.
出版信息
Protein Sci. 2003 Oct;12(10):2379-82. doi: 10.1110/ps.03216203.
Abstract
The rapid binding of cytotoxic colicin E3 by its cognate immunity protein Im3 is essential in safeguarding the producing cell. The X-ray structure of the E3/Im3 complex shows that the Im3 molecule interfaces with both the C-terminal ribonuclease (RNase) domain and the N-terminal translocation domain of E3. The association and dissociation rates of the RNase domain and Im3 show drastically different sensitivities to ionic strength, as previously rationalized for electrostatically enhanced diffusion-limited protein-protein associations. Relative to binding to the RNase domain, binding to full-length E3 shows a comparable association rate but a significantly lower dissociation rate. This outcome is just what was anticipated by a theory for the binding of two linked domains to a protein. The E3/Im3 system thus provides a powerful paradigm for the interplay of theory and experiment.
摘要
细胞毒性大肠杆菌素E3与其同源免疫蛋白Im3的快速结合对于保护产生该毒素的细胞至关重要。E3/Im3复合物的X射线结构表明，Im3分子与E3的C端核糖核酸酶（RNase）结构域和N端转运结构域均有相互作用。RNase结构域与Im3的结合和解离速率对离子强度表现出截然不同的敏感性，正如之前对静电增强的扩散限制型蛋白质-蛋白质相互作用的解释。相对于与RNase结构域的结合，与全长E3的结合表现出相当的结合速率，但解离速率显著更低。这一结果正是两个相连结构域与一种蛋白质结合的理论所预期的。因此，E3/Im3系统为理论与实验的相互作用提供了一个有力的范例。
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