PMID:12831884

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Citation

Rodnina, MV and Wintermeyer, W (2003) Peptide bond formation on the ribosome: structure and mechanism. Curr. Opin. Struct. Biol. 13:334-40

Abstract

The peptidyl transferase reaction on the ribosome is catalyzed by RNA. Pre-steady-state kinetic studies using Escherichia coli ribosomes suggest that catalysis (>10(5)-fold overall acceleration) is, to a large part, a result of substrate positioning, in agreement with crystal structures of large ribosomal subunits with bound substrate or product analogs. The rate of peptide bond formation is inhibited approximately 100-fold by protonation of a single ribosomal group with a pK(a) of 7.5, indicating general acid-base catalysis and/or a pH-dependent conformational change within the active site. According to the kinetics of mutant ribosomes, these effects may be attributed to a candidate catalytic base (A2451) suggested by the crystal structure.

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Keywords

Base Pairing; Binding Sites; Catalysis; Escherichia coli/metabolism; Hydrogen-Ion Concentration; Kinetics; Nucleic Acid Conformation; Peptides/chemistry; Peptides/metabolism; Peptidyl Transferases/metabolism; RNA/metabolism; Ribosomes/chemistry; Ribosomes/metabolism

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