Crystal structure of an initiation factor bound to the 30S ribosomal subunit
2001 | journal article. A publication with affiliation to the University of Göttingen.
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Crystal structure of an initiation factor bound to the 30S ribosomal subunit
Carter, A. P.; Clemons, W. M.; Brodersen, D. E.; Morgan-Warren, R. J.; Hartsch, T.; Wimberly, B. T. & Ramakrishnan, V. (2001)
Science, 291(5503) pp. 498-501. DOI: https://doi.org/10.1126/science.1057766
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Details
- Authors
- Carter, A. P.; Clemons, W. M.; 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.
- Issue Date
- 2001
- Status
- published
- Publisher
- Amer Assoc Advancement Science
- Journal
- Science
- ISSN
- 0036-8075
- Sponsor
- NIGMS NIH HHS [GM 44973]
