首页 | 本学科首页   官方微博 | 高级检索  
   检索      

嗜酸氧化亚铁硫杆菌的谷胱甘肽还原酶的结构模建和底物分子对接
引用本文:刘元东,曾乐平,邱冠周.嗜酸氧化亚铁硫杆菌的谷胱甘肽还原酶的结构模建和底物分子对接[J].现代生物医学进展,2009,9(3).
作者姓名:刘元东  曾乐平  邱冠周
作者单位:1. 中南大学资源加工与生物工程学院,长沙,410083
2. 中南大学雅医院,长沙,410013
3. 中南大学湘雅医学院,长沙,410013
基金项目:,国家重点基础研究发展规划(973计划),国家自然科学基金,the,Mittal,student,Foundation,of,Central,South,University,the,post-graduate,foundation,of,Hunan,province
摘    要:极端环境微生物嗜酸氧化亚铁硫杆菌的谷胱甘肽还原酶(GR)可能在它的抵抗极端酸性,有毒和氧化性的生物浸出环境中发挥至关重要的作用.通过同源模建技术和分子动力学模拟,它的一个三维结构被构建,优化和检验了.获得的结构被进一步用于搜索绑定位点,跟辅因子黄素腺嘌呤二核苷酸(FAD)和底物谷胱甘肽(GSSG)进行分子柔性对接,并以此识别关健残基.对接结果显示,位于活性残基Cys42和Cys47之间的二硫键夹在FAD的活性位点和底物GSSG的二硫键之间.它们之间的距离非常靠近,这跟底物反应机理的初始步骤的情况十分一致.相互作用能表明8个酶中残基Cys42,Cys47,GIu443B,Glu444B,His438B,Ser14,Thr447B和Lys51是固定或激活GSSG的关键残基,这跟以前的实验事实相吻合.此外,根据相互作用能我们还新发现7个重要残基(Arg449B,Pro439B,Thr440B,Thr310,Va143,Gly46 and Va148).所有这些残基在其它物种中的相应物中也都是保守的.这些结果有助于进一步的实验研究和理解其催化机理,进而揭示这种细菌的抗毒机理,服务于工业应用.

关 键 词:谷胱甘肽还原酶  嗜酸氧化亚铁硫杆菌  同源模建  分子动力学  分子对接  黄素腺嘌呤二核苷酸(FAD)  氧化型谷胱甘肽(GSSG)

Homology modeling and substrate binding study of glutathione reductase from Acidithiobacillus ferrooxidans
LIU Yuan-dong,ZENG Le-ping,QIU Guan-zhou.Homology modeling and substrate binding study of glutathione reductase from Acidithiobacillus ferrooxidans[J].Progress in Modern Biomedicine,2009,9(3).
Authors:LIU Yuan-dong  ZENG Le-ping  QIU Guan-zhou
Abstract:Through the homology modeling techniques and molecular dynamics simulations, a 3D model of glutathione reductase was created, refined and checked. The structure obtained was further used to search binding sites, carry out the flexible dockings with the cofactor FAD and the substrate oxidized glutathione disulfide(GSSG), and identify the key residues. The docking results showed that the disulfide bridge between the active residues of Cys42 and Cys47 was sandwiched between the active site of FAD and the disulfide bridge in GSSG. The distance between them was very close, which was well in line with the initial process of substrate reaction mechanism. The interaction energy analysis indicated that the eight residues were key residues for fixing or activating the GSSG; and seven new important residues were first found and identified. All of these residues were conserved in other species. The results may be helpful for further experimental investigation, understanding its catalytic mechanism and subsequently insight into the anti-toxicity of the bacteria could serve for industry.
Keywords:glutathione reductase  docking  FAD  GSSG
本文献已被 CNKI 万方数据 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号