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F1-ATP合酶通过与ATP之间建立广泛的相互作用,实现对ATP的位置进行精确的定位.这些相互作用为ATP的合成/水解创造了稳定的环境.理解这些相互作用是理解ATP的合成/水解机理的基础.我们通过分子动力学模拟方法研究这些相互作用,找出在稳定化过程中起到重要作用的残基.通过检测ATP和F1-ATP合酶之间的非键相互作用,发现残基段158–164所形成的loop区域及残基R189,Y345对ATP存在显著相互作用.其中,该loop区域对ATP的三磷酸部分形成一个半包围结构,封闭活性位点区域,并通过氢键网络约束ATP三磷酸的运动,为ATP合成/水解创造稳定的环境.此外,关键残基Y345通过π–π叠加相互作用对ATP的碱基进行约束,但是ATP的碱基可以在平行于Y345芳香环的平面内进行滑动,我们推断这种滑动运动有利于促进ATP的水解.
The F1-ATP synthase enables precise positioning of ATP positions by establishing extensive interactions with ATP These interactions create a stable environment for the synthesis / hydrolysis of ATP Understanding these interactions is to understand the synthesis of ATP / Hydrolysis mechanism of the basis.We molecular dynamics simulation method to study these interactions, to find out the stabilizing process plays an important role in residues.By detecting ATP and F1-ATP synthase non-key interactions, It was found that the loop region formed by residues 158-164 and the residues R189 and Y345 have a significant interaction with ATP, in which the loop region forms a semi-enclosed structure for the triphosphate moiety of ATP and blocks the active site region Hydrogen-bonded networks constrain the ATP triphosphate movement to create a stable environment for ATP synthesis / hydrolysis.In addition, the key residue Y345 binds the ATP bases through a π-π stacking interaction, but the bases of ATP can be found in parallel Y345 aromatic ring in the plane of sliding, we conclude that this sliding movement is conducive to promoting the hydrolysis of ATP.