Science · 2001 · 379 citations · 39 references
Life SciencesBiochemistryMolecular BiologyProtein TranslationStructural BiologyStructural BiophysicsProtein StructureProtein SynthesisRibosome StructureRna StructureTranslation In ProkaryotesTranslation InitiationBacterial Protein SynthesisInitiation Factor RecruitmentProkaryotic Initiation FactorsProkaryotic Translation Initiation FactorsRibosomal Conformational ChangesRibosome Biogenesis In ProkaryotesSubunit AssociationTranslation Initiation Complexes
Initiation of translation at the correct position on messenger RNA is essential for accurate protein synthesis. In prokaryotes, this process requires three initiation factors: IF1, IF2, and IF3. Here we report the crystal structure of a complex of IF1 and the 30S ribosomal subunit. Binding of IF1 occludes the ribosomal A site and flips out the functionally important bases A1492 and A1493 from helix 44 of 16S RNA, burying them in pockets in IF1. The binding of IF1 causes long-range changes in the conformation of H44 and leads to movement of the domains of 30S with respect to each other. The structure explains how localized changes at the ribosomal A site lead to global alterations in the conformation of the 30S subunit.
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Structure of the 30S ribosomal subunit
Brian T. Wimberly, Ditlev E. Brodersen, William Clemons et al. · Nature · 2000 · 2K citations