Crystal structure of an initiation factor bound to the 30S ribosomal subunit.
Article Details
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Carter AP, Clemons WM Jr, Brodersen DE, Morgan-Warren RJ, Hartsch T, Wimberly BT, Ramakrishnan V
Crystal structure of an initiation factor bound to the 30S ribosomal subunit.
Science. 2001 Jan 19;291(5503):498-501.
- PubMed ID
- 11228145 [ View in PubMed]
- 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.
DrugBank Data that Cites this Article
- Polypeptides
Name UniProt ID 30S ribosomal protein S10 Q5SHN7 Details 30S ribosomal protein S12 Q5SHN3 Details 30S ribosomal protein S11 P80376 Details 30S ribosomal protein S13 P80377 Details 30S ribosomal protein S15 Q5SJ76 Details 30S ribosomal protein S16 Q5SJH3 Details 30S ribosomal protein S18 Q5SLQ0 Details 30S ribosomal protein S19 Q5SHP2 Details 30S ribosomal protein S20 P80380 Details 30S ribosomal protein S4 P80373 Details 30S ribosomal protein S5 Q5SHQ5 Details 30S ribosomal protein S6 Q5SLP8 Details 30S ribosomal protein S7 P17291 Details 30S ribosomal protein S9 P80374 Details 30S ribosomal protein Thx Q5SIH3 Details 30S ribosomal protein S2 P80371 Details 30S ribosomal protein S3 P80372 Details 30S ribosomal protein S14 type Z P0DOY6 Details 30S ribosomal protein S17 P0DOY7 Details 30S ribosomal protein S8 P0DOY9 Details