期刊
SCIENCE
卷 291, 期 5503, 页码 498-501出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1057766
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资金
- NIGMS NIH HHS [GM 44973] Funding Source: Medline
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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