title: Recognition of cognate transfer RNA by the 30S ribosomal subunit.
abstract: 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.
authors.affiliation: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
authors.forename: J M
authors.initials: JM
authors.lastname: Ogle
authors.forename: D E
authors.initials: DE
authors.lastname: Brodersen
authors.forename: W M
authors.initials: WM
authors.lastname: Clemons
authors.forename: M J
authors.initials: MJ
authors.lastname: Tarry
authors.forename: A P
authors.initials: AP
authors.lastname: Carter
authors.forename: V
authors.initials: V
authors.lastname: Ramakrishnan
mesh_terms: D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology; D000926:Anticodon / Q000737:chemistry / Q000378:metabolism; D020029:Base Pairing; D001665:Binding Sites; D003062:Codon / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D006160:Guanosine Triphosphate / Q000378:metabolism; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D010303:Paromomycin / Q000378:metabolism / Q000494:pharmacology; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu / Q000378:metabolism; D014176:Protein Biosynthesis; D012329:RNA, Bacterial / Q000737:chemistry / Q000378:metabolism; D012333:RNA, Messenger / Q000737:chemistry / Q000378:metabolism*; D012336:RNA, Ribosomal, 16S / Q000737:chemistry / Q000378:metabolism*; D012343:RNA, Transfer / Q000737:chemistry / Q000378:metabolism*; D012345:RNA, Transfer, Amino Acid-Specific / Q000737:chemistry / Q000378:metabolism*; D012360:RNA, Transfer, Phe / Q000737:chemistry / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D013816:Thermodynamics; D016963:Thermus thermophilus / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*
chemical_list: D000900:Anti-Bacterial Agents; D000926:Anticodon; D003062:Codon; D012329:RNA, Bacterial; D012333:RNA, Messenger; D012336:RNA, Ribosomal, 16S; D012345:RNA, Transfer, Amino Acid-Specific; D012360:RNA, Transfer, Phe; D010303:Paromomycin; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D010444:Peptide Elongation Factor Tu