1N33
Structure of the Thermus thermophilus 30S ribosomal subunit bound to codon and near-cognate transfer rna anticodon stem-loop mismatched at the second codon position at the a site with paromomycin
Summary for 1N33
| Entry DOI | 10.2210/pdb1n33/pdb |
| Related | 1FJG 1IBK 1IBL 1IBM 1J5E 1N32 1N34 1N36 |
| Descriptor | 16S RIBOSOMAL RNA, 30S RIBOSOMAL PROTEIN S8, 30S RIBOSOMAL PROTEIN S9, ... (26 entities in total) |
| Functional Keywords | 30s ribosomal subunit, ribosome, a site, decoding, near-cognate, mismatch, wobble, gu, g:u, transfer rna, trna, anticodon, stem-loop, messenger rna, mrna, codon, antibiotic, paromomycin |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 23 |
| Total formula weight | 793098.41 |
| Authors | Ogle, J.M.,Murphy IV, F.V.,Tarry, M.J.,Ramakrishnan, V. (deposition date: 2002-10-25, release date: 2002-11-29, Last modification date: 2011-07-13) |
| Primary citation | Ogle, J.M.,Murphy IV, F.V.,Tarry, M.J.,Ramakrishnan, V. Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form Cell(Cambridge,Mass.), 111:721-732, 2002 Cited by PubMed Abstract: A structural and mechanistic explanation for the selection of tRNAs by the ribosome has been elusive. Here, we report crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at the decoding center and compare affinities of equivalent complexes in solution. In ribosomal interactions with near-cognate tRNA, deviation from Watson-Crick geometry results in uncompensated desolvation of hydrogen-bonding partners at the codon-anticodon minor groove. As a result, the transition to a closed form of the 30S induced by cognate tRNA is unfavorable for near-cognate tRNA unless paromomycin induces part of the rearrangement. We conclude that stabilization of a closed 30S conformation is required for tRNA selection, and thereby structurally rationalize much previous data on translational fidelity. PubMed: 12464183DOI: 10.1016/S0092-8674(02)01086-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.35 Å) |
Structure validation
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