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4UJD

mammalian 80S HCV-IRES initiation complex with eIF5B PRE-like state

This is a non-PDB format compatible entry.
Summary for 4UJD
Entry DOI10.2210/pdb4ujd/pdb
Related4UPZ 4UQ0 4UQ1 4UQ4
EMDB information2682
Descriptor28S Ribosomal RNA, 60S RIBOSOMAL PROTEIN L7A, 60S RIBOSOMAL PROTEIN L9, ... (85 entities in total)
Functional Keywordsribosome, translation initiation, hepatitis c virus internal ribosome entry site, eukaryotic initiation factor 5b
Biological sourceORYCTOLAGUS CUNICULUS (RABBIT)
More
Total number of polymer chains83
Total formula weight4044602.91
Authors
Yamamoto, H.,Unbehaun, A.,Loerke, J.,Behrmann, E.,Marianne, C.,Burger, J.,Mielke, T.,Spahn, C.M.T. (deposition date: 2014-06-18, release date: 2014-07-30, Last modification date: 2024-10-23)
Primary citationYamamoto, H.,Unbehaun, A.,Loerke, J.,Behrmann, E.,Marianne, C.,Burger, J.,Mielke, T.,Spahn, C.M.T.
Structure of the Mammalian 80S Initiation Complex with Eif5B on Hcv Ires
Nat.Struct.Mol.Biol., 21:721-, 2014
Cited by
PubMed 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.
PubMed: 25064512
DOI: 10.1038/NSMB.2859
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8.9 Å)
Structure validation

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数据于2025-06-11公开中

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