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Unraveling the Role of Phe82 and Phe351 in Auxin-induced Substrate Perception by TIR1 Ubiquitin Ligase

机译:揭示Phe82和Phe351在TIR1泛素连接酶诱导的生长素诱导的底物感知中的作用

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@@ It is well known that Auxin plays a key role in controlling many aspects of plant growth and development. Crystal structures of Transport inhibitor response 1 (TIR1), a true receptor of auxin, were very recently determined for TIR1 alone and in complexes with auxin and different synthetic analogues and an Auxin/Indole-3-Acetic Acid (Aux/IAA) substrate peptide. However, the dynamic conformational changes of the key residues of TIR1 that take place during the auxin and substrate perception by TIR1 and the detailed mechanism of these changes are still unclear. In the present study, various computational techniques were integrated to uncover the detailed molecular mechanism of the auxin and Aux/IAA perception process; these simulations included molecular dynamics (MD) simulations on complexes and the free enzyme, the molecular mechanics Poisson Boltzmann surface area (MM-PBSA) calculations, normal mode analysis, and hydrogen bond energy (HBE) calculations.
机译:@@众所周知,生长素在控制植物生长和发育的许多方面起着关键作用。最近确定了单独的TIR1以及与生长素和不同的合成类似物以及Auxin / Indole-3-乙酸(Aux / IAA)底物肽复合的TIR1的运输抑制剂反应1(TIR1)的晶体结构,它是生长素的真正受体。 。然而,尚不清楚在生长素和底物被TIR1感知期间TIR1关键残基的动态构象变化以及这些变化的详细机理。在本研究中,整合了各种计算技术以揭示生长素和Aux / IAA感知过程的详细分子机制;这些模拟包括对复合物和游离酶的分子动力学(MD)模拟,泊松玻尔兹曼表面积(MM-PBSA)分子力学计算,正态分析和氢键能(HBE)计算。

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