The structural basis of ribosome activity in peptide bond synthesis.

@article{Nissen2000TheSB,
  title={The structural basis of ribosome activity in peptide bond synthesis.},
  author={Poul Nissen and Jeffrey L Hansen and Nenad Ban and Peter B Moore and Thomas A. Steitz},
  journal={Science},
  year={2000},
  volume={289 5481},
  pages={
          920-30
        }
}
Using the atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with two substrate analogs, we establish that the ribosome is a ribozyme and address the catalytic properties of its all-RNA active site. Both substrate analogs are contacted exclusively by conserved ribosomal RNA (rRNA) residues from domain V of 23S rRNA; there are no protein side-chain atoms closer than about 18 angstroms to the peptide bond being synthesized. The mechanism of peptide bond… 

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Biochemical, genetic and structural evidence highlight the role of the ribosome as an entropic catalyst that accelerates peptide bond formation primarily by substrate positioning and suggests that peptide release should more strongly depend on chemical catalysis likely involving an rRNA group of the PTC.

Ribosomal crystallography: peptide bond formation, chaperone assistance and antibiotics activity.

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Comparisons of high-resolution structures of complexes of antibiotics bound to ribosomes from eubacteria resembling pathogens, to an archaeon that shares properties with eukaryotes and to its mutant that allows antibiotics binding demonstrated the unambiguous difference between mere binding and therapeutical effectiveness.

A structural view on the mechanism of the ribosome-catalyzed peptide bond formation.

...

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