现代食品科技2017，Vol.33Issue(4)：73-81,9.DOI:10.13982/j.mfst.1673-9078.2017.4.012
脱氮硫杆菌硫转移酶SoxAX的建模及分子对接
Threading Modeling and Molecular Docking for Sulfur Oxidation Protein SoxAX of Thiobacillus denitrificans
摘要
Abstract
The sulfur oxidizing (Sox) enzyme complex plays a vital role in the sulfur metabolism of Thiobacillus denitrificans (Td),with the SoxAXYZB complex enzyme at its core.Inorganic sulfur compound substrates need to be successfully combined on the SoxAX complex and transferred to the carrier SoxYZ for further subsequent sulfur oxidation.However,the three-dimensional (3D) structure of Td SoxAX has not yet been elucidated.The protein threading method was adopted in this study in order to construct the Td SoxAX dimer,and the result was verified.Differences in the configuration and energy of binding between the SoxAX protein model and the substrates thiosulfate,hydrogen sulfide,and sulfite were then explored using molecular docking experiments.The result shows that the 3D structure of the constructed SoxAX dimer was relatively reliable.Hydrogen bonds were the major forces that maintained the interaction between SoxA and SoxX.Ten short and strong hydrogen bonds and one pi-pi interaction were involved in stabilizing the dimer structure,and six residues including Arg160 in SoxA and eight residues including Asn15 in SoxX played an important role in the stability of the dimer.Molecular docking studies showed that hydrogen bonds were the major force maintaining the binding between SoxAX and the three different substrates.The key residues for substrate binding were Arg210,Cys214,and Gln217.Among the three substrates,sulfide showed the highest binding energy,followed by thiosulfate and sulfite.关键词
脱氮硫杆菌/Sox蛋白/反向折叠建模/分子对接Key words
Thiobacillus denitrificans/SoxAX cytochromes/threading modeling/molecular docking引用本文复制引用
孟志忠,陆远芳,陈新,罗义,李杉..脱氮硫杆菌硫转移酶SoxAX的建模及分子对接[J].现代食品科技,2017,33(4):73-81,9.基金项目
广东省自然科学基金项目(2016A030313457) （2016A030313457）
