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首页> 外文期刊>Journal of Molecular Biology >Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state.
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Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state.

机译：Arg149参与将结合蛋白AfProX的低亲和力开放状态转换为其高亲和力，封闭状态。

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摘要

The substrate binding protein AfProX from the Archaeoglobus fulgidus ProU ATP binding cassette transporter is highly selective for the compatible solutes glycine betaine (GB) and proline betaine, which confer thermoprotection to this hyperthermophilic archaeon. A detailed mutational analysis of the substrate binding site revealed the contribution of individual amino acids for ligand binding. Replacement of Arg149 by an Ala residue displayed the largest impact on substrate binding. The structure of a mutant AfProX protein (substitution of Tyr111 with Ala) in complex with GB was solved in the open liganded conformation to gain further insight into ligand binding. In this crystal structure, GB is bound differently compared to the GB closed liganded structure of the wild-type AfProX protein. We found that a network of amino acid side chains communicates the presence of GB toward Arg149, which increases ligand affinity and induces domain closure of AfProX. These results were corroborated by molecular dynamics studies and support the view that Arg149 finalizes the high-affinity state of the AfProX substrate binding protein.
机译：来自始祖古细菌ProU ATP结合盒转运蛋白的底物结合蛋白AfProX对相容性溶质甘氨酸甜菜碱（GB）和脯氨酸甜菜碱具有高度选择性，从而赋予该超嗜热古细菌以热保护作用。对底物结合位点的详细突变分析揭示了各个氨基酸对配体结合的贡献。用Ala残基替代Arg149对底物结合的影响最大。突变的AfProX蛋白（Tyr111被Ala取代）与GB的复合结构以开放的配体构象解决，以进一步了解配体结合。在此晶体结构中，与野生型AfProX蛋白的GB封闭配体结构相比，GB的结合方式不同。我们发现，氨基酸侧链的网络将GB的存在传达给Arg149，这会增加配体亲和力并诱导AfProX的域封闭。分子动力学研究证实了这些结果，并支持Arg149最终确定AfProX底物结合蛋白的高亲和力状态的观点。

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