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1IBK

STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTIC PAROMOMYCIN

Summary for 1IBK
Entry DOI10.2210/pdb1ibk/pdb
Related1FJF 1FJG 1IBL 1IBM
Descriptor16S RIBOSOMAL RNA, 30S RIBOSOMAL PROTEIN S9, 30S RIBOSOMAL PROTEIN S10, ... (25 entities in total)
Functional Keywords30s ribosomal subunit, ribosome, antibiotic, paromomycin, aminoglycoside, decoding
Biological sourceThermus thermophilus
More
Total number of polymer chains22
Total formula weight788833.81
Authors
Ogle, J.M.,Brodersen, D.E.,Clemons Jr., W.M.,Tarry, M.J.,Carter, A.P.,Ramakrishnan, V. (deposition date: 2001-03-28, release date: 2001-05-04, Last modification date: 2022-12-21)
Primary citationOgle, J.M.,Brodersen, D.E.,Clemons Jr., W.M.,Tarry, M.J.,Carter, A.P.,Ramakrishnan, V.
Recognition of cognate transfer RNA by the 30S ribosomal subunit.
Science, 292:897-902, 2001
Cited by
PubMed 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.
PubMed: 11340196
DOI: 10.1126/science.1060612
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.31 Å)
Structure validation

226707

數據於2024-10-30公開中

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