Peptide bond formation on the ribosome: structure and mechanism
2003 | review. A publication with affiliation to the University of Göttingen.
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- Authors
- Rodnina, Marina ; Wintermeyer, Wolfgang
- 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.
- Issue Date
- 2003
- Publisher
- Current Biology Ltd
- Journal
- Current Opinion in Structural Biology
- ISSN
- 0959-440X