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首页> 外文期刊>Molecular cell >Structural basis of the ribosomal machinery for Peptide bond formation, translocation, and nascent chain progression.
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Structural basis of the ribosomal machinery for Peptide bond formation, translocation, and nascent chain progression.

机译:肽键形成,易位和新生链进展的核糖体机器的结构基础。

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摘要

Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3' end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.
机译:tRNA模拟物的晶体结构与Deducoccus radiodurans的大核糖体亚基复合,表明远程相互作用决定了tRNA在肽基转移酶中心(PTC)中的精确定向。 PTC耐受嘌呤霉素衍生物的各种方向,其柔韧性允许肽键形成所需的构象重排。稀疏霉素与A2602结合并改变PTC构象。 H69是连接PTC和解码位点的亚基间桥,也可能参与tRNA的放置和转运。 A位点tRNA的3'端围绕PTC内对称的2倍对称轴螺旋旋转表明肽核键形成,A位到P位易位和新生进入的统一核糖体机制蛋白质进入出口通道。在大的核糖体亚基的所有已知结构中检测到的相似的2倍相关区域表明该机制的普遍性。

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