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首页> 外文期刊>Biochemistry >Ligand-Induced Changes in the Conformational Dynamics of a Bacterial Cytotoxic Endonuclease
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Ligand-Induced Changes in the Conformational Dynamics of a Bacterial Cytotoxic Endonuclease

机译：配体诱导的细菌细胞毒性核酸内切酶构象动力学变化

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Knowledge about the conformational dynamics of a protein is key to understanding its biochemical and biophysical properties.In the present work we investigated the dynamic properties of the enzymatic domain of DNase colicins via time-resolved fluorescence and anisotropy decay analysis in combination with steady-state acrylamide quenching experiments.The dynamic properties of the apoenzyme were compared to those of the E9 DNase ligated to the transition metal ion Zn~2+ and the natural inhibitor Im9.We further investigated the contributions of each of the two tryptophans within the E9 DNase(Trp22 and Trp58)using two single-tryptophan mutants(E9 W22F and E9 W58F).Wild-type E9 DNase,E9 W22F,and E9 W58F,as well as Im9,showed multiple lifetime decays.The time-resolved and steady-state fluorescence results indicated that complexation of E9 DNase with Zn~2+ induces compaction of the E9 DNase structure,accompanied by immobilization of Trp22 along with a reduced solvent accessibility for both tryptophans.Im9 binding resulted in immobilization of Trp22 along with a decrease in the longest lifetime component.In contrast,Trp58 experienced less restriction on complexation of E9 DNase with Im9 and showed an increase in the longest lifetime component.Furthermore,the results point out that the Im9-induced changes in the conformational dynamics of E9 DNase are predominant and occur independently of the Zn~2+-induced conformational effects.
机译：有关蛋白质构象动力学的知识是了解其生化和生物物理特性的关键。在本工作中，我们通过时间分辨荧光和各向异性衰减分析结合稳态丙烯酰胺研究了DNase大肠菌素酶结构域的动态特性。将脱辅酶的动态特性与连接到过渡金属离子Zn〜2 +的E9 DNase和天然抑制剂Im9的动力学特性进行了比较。我们进一步研究了两个色氨酸在E9 DNase（Trp22）中的贡献使用两个单色氨酸突变体（E9 W22F和E9 W58F）和Trp58）。野生型E9 DNase，E9 W22F和E9 W58F以及Im9表现出多次寿命衰减。时间分辨和稳态荧光结果表明，E9 DNase与Zn〜2 +的络合可诱导E9 DNase结构的致密化，并伴有Trp22的固定化以及对两种tr的溶剂可及性降低。 Im9结合导致Trp22的固定化以及最长寿命成分的减少。相反，Trp58对E9 DNase与Im9络合的限制较少，并且显示了最长寿命成分的增加。此外，结果指出Im9诱导的E9 DNase构象动力学变化是主要的，并且独立于Zn〜2 +诱导的构象作用而发生。

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