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首页> 外文期刊>Nature structural biology >Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase
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Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase

机译：两种晶体结构在真核核糖体转位酶中显示出较大的构象变化

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摘要

Two crystal structures of yeast translation elongation factor 2 (eEF2) were determined: the apo form at 2.9 Angstrom resolution and eEF2 in the presence of the translocation inhibitor sordarin at 2.1 Angstrom resolution. The overall conformation of apo eEF2 is similar to that of its prokaryotic homolog elongation factor G (EF-G) in complex with GDR Upon sordarin binding, the three tRNA-mimicking C-terminal domains undergo substantial conformational changes, while the three N-terminal domains containing the nucleotide-binding site form an almost rigid unit. The conformation of eEF2 in complex with sordarin is entirely different from known conformations observed in crystal structures of EF-G or from cryo-EM studies of EF-G-70S complexes. The domain rearrangements induced by sordarin binding and the highly ordered drug-binding site observed in the eEF2-sordarin structure provide a high-resolution structural basis for the mechanism of sordarin inhibition. The two structures also emphasize the dynamic nature of the ribosomal translocase. [References: 42]
机译：确定了酵母翻译延伸因子2（eEF2）的两个晶体结构：载脂蛋白形式的2.9埃分辨率和eEF2在易位抑制剂索达林存在下的2.1埃分辨率。 apo eEF2的整体构型与其原核同源延伸因子G（EF-G）的相似，与GDR形成复合物sordarin结合后，模仿tRNA的3个C末端结构域发生了实质性构象变化，而3个N末端包含核苷酸结合位点的结构域形成几乎刚性的单元。与sordarin配合物中的eEF2构象与在EF-G晶体结构中观察到的已知构象或从EF-G-70S配合物的冷冻EM研究中完全不同。在eEF2-sordarin结构中观察到的由sordarin结合诱导的结构域重排和高度有序的药物结合位点为sordarin抑制的机理提供了高分辨率的结构基础。这两个结构还强调了核糖体转位酶的动力学性质。 [参考：42]

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