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|1vq6, resolution 2.70Å ()|
|Ligands:||, , , ,|
|Non-Standard Residues:||, , , , , , , ,|
|Related:||1s72, 1jj2, 1kqs, 1m90, 1q7y, 1q81, 1q82, 1q86, 1qvf, 1qvg, 1ffk, 1ffz, 1fgo, 1vq4, 1vq5, 1vq7, 1vq8, 1vq9, 1vqk, 1vql, 1vqm, 1vqn, 1vqo, 1vqp|
The structure of c-hpmn and CCA-PHE-CAP-BIO bound to the large ribosomal subunit of haloarcula marismortui
The large ribosomal subunit catalyses the reaction between the alpha-amino group of the aminoacyl-tRNA bound to the A site and the ester carbon of the peptidyl-tRNA bound to the P site, while preventing the nucleophilic attack of water on the ester, which would lead to unprogrammed deacylation of the peptidyl-tRNA. Here we describe three new structures of the large ribosomal subunit of Haloarcula marismortui (Hma) complexed with peptidyl transferase substrate analogues that reveal an induced-fit mechanism in which substrates and active-site residues reposition to allow the peptidyl transferase reaction. Proper binding of an aminoacyl-tRNA analogue to the A site induces specific movements of 23S rRNA nucleotides 2618-2620 (Escherichia coli numbering 2583-2585) and 2541(2506), thereby reorienting the ester group of the peptidyl-tRNA and making it accessible for attack. In the absence of the appropriate A-site substrate, the peptidyl transferase centre positions the ester link of the peptidyl-tRNA in a conformation that precludes the catalysed nucleophilic attack by water. Protein release factors may also function, in part, by inducing an active-site rearrangement similar to that produced by the A-site aminoacyl-tRNA, allowing the carbonyl group and water to be positioned for hydrolysis.
An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA., Schmeing TM, Huang KS, Strobel SA, Steitz TA, Nature. 2005 Nov 24;438(7067):520-4. PMID:16306996
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Ribosomal protein L10
- Ribosomal protein L11
- Ribosomal protein L13
- Ribosomal protein L14
- Ribosomal protein L2
- Ribosomal protein L3
- Ribosomal protein L5
- Ribosomal protein L6
- Ribosomal protein L7
- Schmeing TM, Huang KS, Strobel SA, Steitz TA. An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature. 2005 Nov 24;438(7067):520-4. PMID:16306996 doi:10.1038/nature04152
- Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA. Structural insights into the roles of water and the 2' hydroxyl of the P site tRNA in the peptidyl transferase reaction. Mol Cell. 2005 Nov 11;20(3):437-48. PMID:16285925 doi:http://dx.doi.org/10.1016/j.molcel.2005.09.006