| Effect of Residue Mutation on the Electrostatic Potential in EcCIC |
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| 作者姓名： | ZOU Xianwu DONG Shuxiang WANG Xiaoqing HUANG Shengyou |
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| 作者单位： | School of Physics and Technology, Wuhan University,Wuhan 430072, Hubei, China |
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| 基金项目： | Supported by the Foundation for the Author of National Excellent Doctoral Dissertation of China（200525） and the Science and Technology Program of Wuhan City（20067003111-07） |
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| 摘 要： | The effect of mutation of strongly conserved porelining residues in the chloride channel EcClC on the electrostatic potential and binding free energy of the chloride ion was studied using explicit protein-membrane structures. Electrostatic potential distribution and binding free energy of the chloride ion at different binding sites in the wild-type and mutated EcClC were calculated with APBS. The potential data reveal that the electrostatic potential around the selectivity filter, especially around the site Sext and Scen becomes more negative as the residue R147 was mutated to C147. The electrostatic binding free energy shows that the binding free energy of the chloride ion at all binding sites becomes more positive as R147 was mutated. It follows that mutation of R147 decreases ion stabilization at binding sites and affects channel＇s gating.
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| 关 键 词： | 静电位势 氯化物 捆绑式能源 突变 |
| 文章编号： | 1007-1202（2007）06-1029-05 |
| 收稿时间： | 27 April 2007 |
| 修稿时间： | 2007-04-27 |
Effect of residue mutation on the electrostatic potential in EcCIC |
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| ZOU Xianwu DONG Shuxiang WANG Xiaoqing HUANG Shengyou.Effect of Residue Mutation on the Electrostatic Potential in EcCIC[J].Wuhan University Journal of Natural Sciences,2007,12(6):1029-1033. |
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| Authors: | Zou Xianwu Dong Shuxiang Wang Xiaoqing Huang Shengyou |
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| Institution: | (1) School of Physics and Technology, Wuhan University, Wuhan, 430072, Hubei, China |
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| Abstract: | The effect of mutation of strongly conserved porelining residues in the chloride channel EcClC on the electrostatic potential
and binding free energy of the chloride ion was studied using explicit protein-membrane structures. Electrostatic potential
distribution and binding free energy of the chloride ion at different binding sites in the wild-type and mutated EcClC were
calculated with APBS. The potential data reveal that the electrostatic potential around the selectivity filter, especially
around the site S
ext and S
cen becomes more negative as the residue R147 was mutated to C147. The electrostatic binding free energy shows that the binding
free energy of the chloride ion at all binding sites becomes more positive as R147 was mutated. It follows that mutation of
R147 decreases ion stabilization at binding sites and affects channel’s gating.
Biography: ZOU Xianwu(1938–), male, Professor, research direction: soft matter. |
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| Keywords: | chloride channel electrostatic potential binding free energy mutation |
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