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

Yamamoto, H.; Unbehaun, A.; Loerke, J.; Behrmann, E.; Collier, M.; Burger, J.; Mielke, T.; Spahn, C. M. T.

doi:10.1038/nsmb.2859

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

http://www.ncbi.nlm.nih.gov/pubmed/25064512
(Any fulltext)

http://www.nature.com/nsmb/journal/v21/n8/pdf/nsmb.2859.pdf
(Any fulltext)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Yamamoto, H., Unbehaun, A., Loerke, J., Behrmann, E., Collier, M., Burger, J., et al. (2014). Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA. Nature structural & molecular biology, 21(8), 721-7. doi:10.1038/nsmb.2859.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-636A-A

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.