Mechanism of tetracycline resistance by ribosomal protection protein Tet(O)
Open Access
- 12 February 2013
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature Communications
- Vol. 4 (1), 1-8
- https://doi.org/10.1038/ncomms2470
Abstract
Tetracycline resistance protein Tet(O), which protects the bacterial ribosome from binding the antibiotic tetracycline, is a translational GTPase with significant similarity in both sequence and structure to the elongation factor EF-G. Here, we present an atomic model of the Tet(O)-bound 70S ribosome based on our cryo-electron microscopic reconstruction at 9.6-Å resolution. This atomic model allowed us to identify the Tet(O)-ribosome binding sites, which involve three characteristic loops in domain 4 of Tet(O). Replacements of the three amino-acid tips of these loops by a single glycine residue result in loss of Tet(O)-mediated tetracycline resistance. On the basis of these findings, the mechanism of Tet(O)-mediated tetracycline resistance can be explained in molecular detail.This publication has 40 references indexed in Scilit:
- Structural basis for TetM-mediated tetracycline resistanceProceedings of the National Academy of Sciences of the United States of America, 2012
- Theoretical and Computational Investigation of Flagellin Translocation and Bacterial Flagellum GrowthBiophysical Journal, 2011
- Molecular dynamics of EF‐G during translocationProteins-Structure Function and Bioinformatics, 2011
- Molecular dynamics flexible fitting: A practical guide to combine cryo-electron microscopy and X-ray crystallographyMethods, 2009
- SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographsNature Protocols, 2008
- Preparation of macromolecular complexes for cryo-electron microscopyNature Protocols, 2007
- Modeling Experimental Image Formation for Likelihood-Based Classification of Electron Microscopy DataStructure, 2007
- Structures of modified eEF2·80S ribosome complexes reveal the role of GTP hydrolysis in translocationThe EMBO Journal, 2007
- Automated acquisition of cryo-electron micrographs for single particle reconstruction on an FEI Tecnai electron microscopeJournal of Structural Biology, 2005
- MAFFT version 5: improvement in accuracy of multiple sequence alignmentNucleic Acids Research, 2005