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      Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA.

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          Abstract

          The universally conserved eukaryotic initiation factor (eIF) 5B, a translational GTPase, is essential for canonical translation initiation. It is also required for initiation facilitated by the internal ribosomal entry site (IRES) of hepatitis C virus (HCV) RNA. eIF5B promotes joining of 60S ribosomal subunits to 40S ribosomal subunits bound by initiator tRNA (Met-tRNAi(Met)). However, the exact molecular mechanism by which eIF5B acts has not been established. Here we present cryo-EM reconstructions of the mammalian 80S-HCV-IRES-Met-tRNAi(Met)-eIF5B-GMPPNP complex. We obtained two substates distinguished by the rotational state of the ribosomal subunits and the configuration of initiator tRNA in the peptidyl (P) site. Accordingly, a combination of conformational changes in the 80S ribosome and in initiator tRNA facilitates binding of the Met-tRNAi(Met) to the 60S P site and redefines the role of eIF5B as a tRNA-reorientation factor.

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          Author and article information

          Journal
          Nat Struct Mol Biol
          Nature structural & molecular biology
          Springer Science and Business Media LLC
          1545-9985
          1545-9985
          Aug 2014
          : 21
          : 8
          Affiliations
          [1 ] 1] Institute of Medical Physics and Biophysics, Charité-Universitätsmedizin, Berlin, Germany. [2].
          [2 ] Institute of Medical Physics and Biophysics, Charité-Universitätsmedizin, Berlin, Germany.
          [3 ] 1] Institute of Medical Physics and Biophysics, Charité-Universitätsmedizin, Berlin, Germany. [2] UltraStrukturNetzwerk, Max Planck Institute for Molecular Genetics, Berlin, Germany.
          Article
          nsmb.2859
          10.1038/nsmb.2859
          25064512
          2e31fdc7-6b94-45a6-a361-96b78bfe63bb

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