On the structural basis of peptide-bond formation and antibiotic resistance from atomic structures of the large ribosomal subunit

Thomas A Steitz

doi:10.1016/j.febslet.2004.11.053

On the structural basis of peptide-bond formation and antibiotic resistance from atomic structures of the large ribosomal subunit

FEBS Lett. 2005 Feb 7;579(4):955-8. doi: 10.1016/j.febslet.2004.11.053.

Author

Thomas A Steitz¹

Affiliation

¹ Department of Molecular Biophysics and Biochemistry, Yale University, and Howard Hughes Medical Institute, P.O. Box 208114, New Haven, CT 06520-8114, USA. eatherton@csb.yale.edu

PMID: 15680981
DOI: 10.1016/j.febslet.2004.11.053

Abstract

The atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with substrates and antibiotics have provided insights into the way the 3000 nucleotide 23S rRNA folds into a compact, specific structure and interacts with 27 ribosomal proteins as well as the structural basis of the peptidyl transferase reaction and its inhibition by antibiotics. The structure shows that the ribosome is indeed a ribozyme.

Publication types

Review

MeSH terms

Anti-Bacterial Agents / chemistry*
Anti-Bacterial Agents / pharmacology
Drug Resistance, Microbial*
Haloarcula marismortui / physiology
Molecular Structure
Nucleic Acid Conformation
Peptide Chain Elongation, Translational / drug effects
Peptide Chain Elongation, Translational / physiology
Peptidyl Transferases / physiology
Protein Biosynthesis* / drug effects
RNA, Ribosomal, 23S / metabolism
RNA, Transfer / metabolism
Ribosomal Proteins / chemistry
Ribosomal Proteins / physiology
Ribosomes / chemistry*
Ribosomes / drug effects*

Substances

Anti-Bacterial Agents
RNA, Ribosomal, 23S
Ribosomal Proteins
RNA, Transfer
Peptidyl Transferases