Journal
SCIENCE
Volume 291, Issue 5503, Pages 498-501Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1057766
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- NIGMS NIH HHS [GM 44973] Funding Source: Medline
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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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