嗜热酯酶EstTs1的远源三维结构模建及分子对接

J4 ›› 2011, Vol. 49 ›› Issue (06): 1131-1135.

嗜热酯酶EstTs1的远源三维结构模建及分子对接

詹冬玲¹, 邵鸿泽¹, 韩葳葳², 刘景圣¹

1. 吉林农业大学食品科学与工程学院, 长春 130118； 2. 吉林大学分子酶学工程教育部重点实验室, 长春 130012

收稿日期:2011-03-09 出版日期:2011-11-26 发布日期:2011-11-28
通讯作者: 刘景圣 E-mail:liujs1007@vip.sina.com.cn

Remote Homology Modeling and Molecular Dockingof Thermostable Esterase (EstTs1)

ZHAN Dongling¹, SHAO Hong ze¹, HAN Weiwei², LIU Jingsheng¹

1. College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China|2. Key Laboratory forMolecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130012, China

Received:2011-03-09 Online:2011-11-26 Published:2011-11-28
Contact: LIU Jingsheng E-mail:liujs1007@vip.sina.com.cn

摘要/Abstract

摘要：

利用Phyre网络服务器, 构建嗜热酯酶EstTs1的三维结构, 并通过分子动力学优化构型, 得到了可靠的构型. 分子对接研究表明, p
硝基苯基丁酸酯是EstTs1的最适底物, 其大小正适合EstTs1的活性口袋. Thr111是底物与酶结合的重要残基, 与底物形成了氢键; Ser85是重要的催化残基.

关键词: 远源三维结构模建；分子对接；嗜热酯酶EstTs1

Abstract:

A 3D structure of thermostable esterase (EstTs1) was built by means of the protein homology/analogy recognition engine (Phyre) program and further refined via unrestrained dynamics simulation. The docking results reveal that p-nitrophenyl butyrate （C₄） is the best substrate of EstTs1, which has the adaptive size to the EstTs1. In addition, the key bindingsite residue of Thr111 plays an important role in the catalysis of EstTs1 for it made a hydrogen bond with p-nitrophenyl butyrate. One important finding was that the identification of the key binding site： residue of Ser85 which plays an important role in the catalysis of EstTs1.

Key words: remote homology modeling, docking, thermostable esterase EsTs1

中图分类号:

O623

詹冬玲, 邵鸿泽, 韩葳葳, 刘景圣. 嗜热酯酶EstTs1的远源三维结构模建及分子对接[J]. J4, 2011, 49(06): 1131-1135.

DAN Dong-Ling, SHAO Hong-Ze, HAN Wei-Wei, LIU Jing-Ku. Remote Homology Modeling and Molecular Dockingof Thermostable Esterase (EstTs1)[J]. J4, 2011, 49(06): 1131-1135.