Recognition of Cognate Transfer RNA by the 30S Ribosomal Subunit

Journal Article · Wed Oct 07 00:00:00 EDT 2009 · Science

DOI:https://doi.org/10.1126/science.1060612· OSTI ID:1006349

Ogle, James M; Brodersen, Ditlev E; Clemons, William M; Tarry, Michael J; Carter, Andrew P; Ramakrishnan, V ^[1]

---

1. MRC Laboratory of Molecular Biology

Crystal structures of the 30S ribosomal subunit in complex with messenger RNA and cognate transfer RNA in the A site, both in the presence and absence of the antibiotic paromomycin, have been solved at between 3.1 and 3.3 angstroms resolution. Cognate transfer RNA (tRNA) binding induces global domain movements of the 30S subunit and changes in the conformation of the universally conserved and essential bases A1492, A1493, and G530 of 16S RNA. These bases interact intimately with the minor groove of the first two base pairs between the codon and anticodon, thus sensing Watson-Crick base-pairing geometry and discriminating against near-cognate tRNA. The third, or 'wobble,' position of the codon is free to accommodate certain noncanonical base pairs. By partially inducing these structural changes, paromomycin facilitates binding of near-cognate tRNAs.

• Research Organization: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: USDOE
• OSTI ID: 1006349
• Journal Information: Science, Vol. 292, Issue 2001; ISSN 0193-4511
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
ANTIBIOTICS
CODONS
CRYSTAL STRUCTURE
GEOMETRY
MESSENGER-RNA
RESOLUTION
RNA
TRANSFER RNA