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- W2091336733 abstract "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." @default.
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- W2091336733 date "2001-01-19" @default.
- W2091336733 modified "2023-10-14" @default.
- W2091336733 title "Crystal Structure of an Initiation Factor Bound to the 30<i>S</i>Ribosomal Subunit" @default.
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- W2091336733 doi "https://doi.org/10.1126/science.1057766" @default.
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