| 拟南芥和酿酒酵母来源的磷脂：甘油二酯酰基转移酶与底物的潜在结合位点分析 |
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| 引用本文： | 王 炼,黄庭轩,罗 玲,万 霞.拟南芥和酿酒酵母来源的磷脂：甘油二酯酰基转移酶与底物的潜在结合位点分析[J].中国油料作物学报,2018,40(6):812. |
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| 作者姓名： | 王 炼 黄庭轩 罗 玲 万 霞 |
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| 作者单位： | １．中国农业科学院油料作物研究所，湖北武汉，４３００６２；
２．农业部油料作物生物学与遗传育种重点实验室，湖北武汉，４３００６２；
３．油料油脂加工技术国家地方联合工程实验室，湖北武汉，４３００６２；
４．油料脂质化学与营养湖北省重点实验室，湖北武汉，４３００６２ |
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| 基金项目： | 中国农业科学院科技创新工程（CAAS-ASTIP-2013-OCRI）；十三五重点研发计划( 2016YFD0501209-01) |
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| 摘 要： | 为了探究拟南芥和酿酒酵母来源的磷脂:甘油二酯酰基转移酶（PDAT）在油脂积累过程中与底物相互作用的机制，本研究利用蛋白三维结构模拟、分子对接等生物信息学手段对植物、真菌等来源的PDAT进行蛋白进化分析以及PDAT与特定底物的分子对接分析。通过模拟PDAT和磷脂分子的空间对接模型，预测出底物和蛋白空间互作的多个关键氨基酸位点。基于多种磷脂分子和AtPDAT的分子对接和氨基酸序列比对，AtPDAT氨基酸序列中的W153，E310，D313，V627可能对蛋白质和底物结合发挥重要作用。该结果精确定位PDAT与磷脂底物的结合位点以及催化位点，为下一步PDAT蛋白定向改造提供重要的数据支撑。
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| 关 键 词： | 拟南芥 酿酒酵母 磷脂：甘油二酯酰基转移酶 磷脂 分子对接 |
Analysis of potential substrate binding sites of PDAT in Arabidopsis thaliana and Saccharomyces cerevisiae |
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| WANG Lian,HUANG Ting-xuan,LUO Ling,WAN Xia.Analysis of potential substrate binding sites of PDAT in Arabidopsis thaliana and Saccharomyces cerevisiae[J].Chinese Journal of Oil Crop Sciences,2018,40(6):812. |
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| Authors: | WANG Lian HUANG Ting-xuan LUO Ling WAN Xia |
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| Institution: | 1.Oil Crops Research Institute of Chinese Academy of Agricultural Sciences ，Wuhan 430062，China;
2. Key Laboratory of Biology and Genetic Improvement of Oil Crops，Ministry of Agriculture，Wuhan 430062，China;
3．National and Local Joint Engineering Laboratory of Oil Lipid Processing Technology，Wuhan 430062，China;
4．Hubei Key Laboratory of Lipid Chemistry and Nutrition，Wuhan 430062，China |
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| Abstract: | To explore the interaction mechanism between substrate and phospholipid: diacylglycerol acyltransferases (PDATs) in Arabidopsis thaliana and Saccharomyces cerevisiae, phylogenetic relationships of PDAT in plants, fungi, and other species were investigated by bioinformatics approaches including three-dimensional structure simulation and molecular docking. The binding model between PDAT and specific phospholipid was created by molecular docking. The key amino acids of intermolecular interactions between phospholipid substrate and PDAT were then predicted. Amino acids including W153，E310，D313，V627 in protein sequences of AtPDAT might have played an important role in substrate-binding domain on the base of molecular docking between several phospholipids of AtPDAT and sequence alignment of PDAT proteins. This result accurately revealed the binding site of substrate to PDAT as well as the catalytic domain of candidate PDATs, and provided guidance for future improvement of PDATs. |
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| Keywords: | Arabidopsis thaliana Saccharomyces cerevisiae PDAT phospholipids molecular docking |
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