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TitleStructural roles for human translation factor eIF3 in initiation of protein synthesis.
Journal, issue, pagesScience, Vol. 310, Issue 5753, Page 1513-1515, Year 2005
Publish dateDec 2, 2005
AuthorsBunpote Siridechadilok / Christopher S Fraser / Richard J Hall / Jennifer A Doudna / Eva Nogales /
PubMed AbstractProtein synthesis in mammalian cells requires initiation factor eIF3, a approximately 750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either ...Protein synthesis in mammalian cells requires initiation factor eIF3, a approximately 750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5'-cap or an internal ribosome entry site (IRES). Cryo-electron microscopy reconstructions show that eIF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5'-cap binding complex eIF4F via the same domain. Detailed modeling of eIF3 and eIF4F onto the 40S ribosomal subunit reveals that eIF3 uses eIF4F or the HCV IRES in structurally similar ways to position the mRNA strand near the exit site of 40S, promoting initiation complex assembly.
External linksScience / PubMed:16322461
MethodsEM (single particle)
Resolution33.0 - 40.0 Å
Structure data

EMDB-1170:
Structural roles for human translation factor eIF3 in initiation of protein synthesis.
Method: EM (single particle) / Resolution: 33.0 Å

EMDB-1171:
Structural roles for human translation factor eIF3 in initiation of protein synthesis.
Method: EM (single particle) / Resolution: 40.0 Å

Source
  • Homo sapiens (human)

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