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- Title
Crystal structure of an initiation factor bound to the 30S ribosomal subunit.
- Authors
Carter, A P; Clemons, W M, Jr; Brodersen, D E; Morgan-Warren, R J; Hartsch, T; Wimberly, B T; Ramakrishnan, V
- 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.
- Publication
Science (New York, N.Y.), 2001, Vol 291, Issue 5503, p498
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.1057766