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|1vq8, resolution 2.20Å (default scene)|
|Ligands:||CD, CL, K, MG, NA, SPS, SR|
|Non-Standard Residues:||1MA, ACA, OMG, OMU, PSU, UR3|
|Related:||1s72, 1jj2, 1kqs, 1m90, 1q7y, 1q81, 1q82, 1q86, 1qvf, 1qvg, 1ffk, 1ffz, 1fgo, 1vq4, 1vq5, 1vq6, 1vq7, 1vq9, 1vqk, 1vql, 1vqm, 1vqn, 1vqo, 1vqp|
The structure of CCDA-PHE-CAP-BIO and the antibiotic sparsomycin bound to the large ribosomal subunit of haloarcula marismortui
Peptide bond formation is catalyzed at the peptidyl transferase center (PTC) of the large ribosomal subunit. Crystal structures of the large ribosomal subunit of Haloarcula marismortui (Hma) complexed with several analogs that represent either the substrates or the transition state intermediate of the peptidyl transferase reaction show that this reaction proceeds through a tetrahedral intermediate with S chirality. The oxyanion of the tetrahedral intermediate interacts with a water molecule that is positioned by nucleotides A2637 (E. coli numbering, 2602) and (methyl)U2619(2584). There are no Mg2+ ions or monovalent metal ions observed in the PTC that could directly promote catalysis. The A76 2' hydroxyl of the peptidyl-tRNA is hydrogen bonded to the alpha-amino group and could facilitate peptide bond formation by substrate positioning and by acting as a proton shuttle between the alpha-amino group and the A76 3' hydroxyl of the peptidyl-tRNA.
Structural insights into the roles of water and the 2' hydroxyl of the P site tRNA in the peptidyl transferase reaction., Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA, Mol Cell. 2005 Nov 11;20(3):437-48. PMID:16285925
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