Structural determinants of V. cholerae CheYs that discriminate them in FliM binding:: Comparative modeling and MD simulation studies
Structural determinants of V. cholerae CheYs that discriminate them in FliM binding:: Comparative modeling and MD simulation studies
复制标题
DOI：
10.1080/07391102.2008.10507196
复制
发表时间：
2008-04-01
影响因子：
4.4
通讯作者：
Dattagupta, Jiban K.
中科院分区：
文献类型：
--
作者：
Dasgupta, Jhimli;Dattagupta, Jiban K.
霍乱弧菌的趋化性是一个复杂的过程，其中多种趋化性基因的多个旁系同源物参与。霍乱弧菌含有五个拷贝的反应调节蛋白CheY（CheY（v）），这些CheY同源物在趋化性和毒力中所起的作用仅通过少数体内研究进行了研究。由于鉴别在FliM结合方面区分CheY（v）s的分子特征对于详细理解趋化性和发病机制是必要的，我们通过比较建模建立了CheY（v）s的模型，并在磷酸化和Mg+2结合状态下对每个模型进行了MD模拟。我们的分析确定了CheY 3（v）特有的关键结构元件，这些元件补充了FliM（v）的N-末端部分，我们解释了其他CheY（v）的FliM结合口袋的结构，形状和表面性质如何废除这一功能。此外，我们还提供了在最近的体内研究中鉴定的CheY（E）和FliM（v）之间的假定跨物种相互作用的结构基础。
Chemotaxis of Vibrio cholerae is a complex process where multiple paralogues of various chemotaxis genes participate. V. cholerae contains five copies of the response regulator protein CheY (CheY(v)) and the role played by these CheY homologs in chemotaxis and virulence are investigated only through a few in vivo studies. As identification of the molecular features that discriminate CheY(v)s in terms of FliM binding is necessary for the detailed understanding of chemotaxis and pathogenesis, we built the models of CheY(v)s through comparative modeling and MD simulation was performed on each model in their phosphorylated and Mg+2 bound state. Our analysis identified the key structural elements, unique to CheY3(v), which complement the N-terminal part of FliM(v) and we explained how the structure, shape, and surface properties of the FliM binding pocket of other CheY(v)s abrogate this function. Furthermore, we have provided the structural basis of a putative cross species interaction between CheY(E) and FliM(v), identified in a recent in vivo study.