title: The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A.
abstract: Eukaryotic translation initiation factors (eIFs) 1A and 1 are central players in the complex process of start-codon recognition. To improve mechanistic understanding of this process, we determined the crystal structure of the 40S ribosomal subunit in complex with eIF1A and eIF1 from Tetrahymena thermophila at a resolution of 3.7 Å. It reveals the positions of the two factors on the 40S and the conformational changes that accompany their binding.
authors.affiliation: Institute of Molecular Biology and Biophysics, Swiss Federal Institute of Technology (ETH Zürich), Zürich, Switzerland.
authors.forename: Melanie
authors.initials: M
authors.lastname: Weisser
authors.forename: Felix
authors.initials: F
authors.lastname: Voigts-Hoffmann
authors.forename: Julius
authors.initials: J
authors.lastname: Rabl
authors.forename: Marc
authors.initials: M
authors.lastname: Leibundgut
authors.forename: Nenad
authors.initials: N
authors.lastname: Ban
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D039642:Eukaryotic Initiation Factors / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry*; D011487:Protein Conformation; D054682:Ribosome Subunits, Small, Eukaryotic / Q000737:chemistry*; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D016808:Tetrahymena thermophila / Q000737:chemistry*
chemical_list: D039642:Eukaryotic Initiation Factors; D046912:Multiprotein Complexes