八氢番茄红素脱氢酶的分子结构及其与达草灭相互作用分析

The molecular structure of Phytoene desaturase and the analysis of the interaction between PDS and norflurazon

摘要:

八氢番茄红素脱氢酶（Phytoene desaturase，PDS）是除草剂达草灭的靶点，本文对野生型和两种突变型八氢番茄红素脱氢酶的二维和三维结构进行预测，并通过DOCK6.5进行八氢番茄红素脱氢酶与达草灭的分子对接比较，利用 Gromacs进行分子动力学模拟，分析其与达草灭的结合稳定性，使用Amber9中的mm_pbsa.pl工具分析能量分布及变化.LIGPLOT+软件进行氢键分析确认结合氨基酸位点. 结果发现突变对二维和三维结构无影响，但是在达草灭存在的情况下，突变的PDS有更高的结合能以及更弱的结合稳定性，更难以与达草灭结合，阐明抗性产生的机理.

Abstract:

Phytoene desaturase(PDS) is the target of the bleaching herbicide,norflurazon.The the 2D and 3D structures of wild PDS and two mutations were achived by online prediction,docking of PDS and norflurazon was carried out by DOCK6.5.Binding stablity was analysed by molecular dynamics simulation via the software Gromacs.The energy changes and distribution were revealed by mm_pbsa.pl tools in Amber9.At last,important amino acids were confirmed by the analysis of hydrogen bond with LIGPLOT+. The results suggested that different mutations didn’t change the 2D and 3D structures of PDS,but mutated PDS showed higher RMSD,which indicated lower binding stablity,and higher bingding energy,which indicated the difficulity to bind to noflurazon .Our research might explain the mechanisms of the resistance to norflurazon.