肠膜明串珠菌二鸟苷酸环化酶生物信息学分析  

Bioinformatics analysis of the diguanylate cyclase of Leuconostoc mesenteroides

作　　者：李腾鑫 于连升 周渤森 杨义 杜仁鹏 LI Tengxin;YU Liansheng;ZHOU Bosen;YANG Yi;DU Renpeng(Engineering Research Center of Agricultural Microbiology Technology,Ministry of Education/Heilongjiang Provincial Key Laboratory of Plant Genetic Engineering and Biological Fermentation Engineering for Cold Region/Key Laboratory of Microbiology,College of Heilongjiang Province,School of Life Sciences,Heilongjiang University,Harbin 150080,China;Hebei Key Laboratory of Agroecological Safety,Hebei University of Environmental Engineering,Qinhuangdao 066102,China)

机构地区：[1]黑龙江大学生命科学学院农业微生物技术教育部工程研究中心/黑龙江省寒区植物基因与生物发酵重点实验室/黑龙江省普通高校微生物重点实验室,哈尔滨150080 [2]河北环境工程学院河北省农业生态安全重点实验室,秦皇岛066102

出　　处：《黑龙江大学自然科学学报》2024年第4期453-462,共10页Journal of Natural Science of Heilongjiang University

基　　金：黑龙江省自然科学基金优秀青年基金资助项目(YQ2021C030);中国博士后科学基金资助项目(2022MD713755);黑龙江省博士后科学基金资助项目(LBH-Z21082);“新时代龙江优秀硕士、博士学位论文”资助项目(LJYXL2022-020);河北省农业生态安全重点实验室开放基金资助项目(2023SYSJJ17);黑龙江省省属高等学校基本科研业务费项目(2022-KYYWF-1075)。

摘　　要：环二鸟苷酸(Cyclic diguanosine monophosphate,c-di-GMP)可以调控细菌的生存优势,从而使细菌适应环境的改变。二鸟苷酸环化酶(Diguanylate cyclase,DGC)可以通过催化2个GTP分子合成c-di-GMP,虽然不同来源的DGC的催化功能类似,但是催化方式及调控通路存在较大差异,因此表征新来源的DGC具有重要的意义。以肠膜明串珠菌(Leuconostoc mesenteroides,Ln.mesenteroides)DRP105中的DGC序列为基础,进行了生物信息学分析。结果表明,DGC含有5个开放阅读框和1个保守结构域,并且与Ln.mesenteroides CBA3607中含有GGDEF结构域的蛋白高度相似。理化性质分析结果表明,DGC是一种定位于细胞膜上的亲水蛋白,存在6段跨膜螺旋结构。结构预测结果显示,DGC含有3段保守序列,主要由α-螺旋和β-折叠组成,含有GGEEF结构域和Mg 2+结合位点。分子对接结果表明,2个GTP分子与c-di-GMP的活性口袋稳定结合。本研究结果可为后续深入探索Ln.mesenteroides DGC的催化功能提供理论基础。Cyclic diguanosine monophosphata(c-di-GMP)can regulate the survival advantage of bacteria,so that bacteria can adapt to environmental changes.Diguanylate cyclase(DGC)can catalyze the synthesis of c-di-GMP from 2 GTP molecules.Although the catalytic functions of different sources of DGC are similar,there are major differences in the catalytic mode and regulatory pathways,and it is important to characterize new sources of DGC.The DGC sequence in Leuconostoc mesenteroides(Ln.mesenteroides)was therefore used as the basis for bioinformatics analysis.The results show that DGC contains five open reading frames,one conserved structural domain and is highly similar to the GGDEF domain of Ln.mesenteroides.The results of the physicochemical analysis show that DGC is a hydrophilic protein localized to the cell membrane,with a six-segment transmembrane helix structure.Structural prediction and molecular docking show that DGC contains 3 conserved sequences,mainly consisting ofα-helices andβ-folds,a GGEEF domain and a Mg 2+binding site.Molecular docking shows that 2 GTP molecules are stably bound to the active pocket of c-di-GMP.The results of this experiment provide a preliminary basis for subsequent deeper exploration of the catalytic function of DGC in Ln.mesenteroides.

关 键 词：肠膜明串珠菌 二鸟苷酸环化酶 生物信息学分析 结构预测 分子对接 

分 类 号：Q819[生物学—生物工程]