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Mechanism of tetracycline resistance by ribosomal protection protein Tet(O)

Li, Wen LU ; Atkinson, Gemma C. LU orcid ; Thakor, Nehal S. ; Allas, Ular ; Lu, Chuao Chao ; Yan Chan, Kwok ; Tenson, Tanel ; Schulten, Klaus ; Wilson, Kevin S. and Hauryliuk, Vasili LU orcid , et al. (2013) In Nature Communications 4. p.1-8
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... (More)

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.

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publishing date
type
Contribution to journal
publication status
published
in
Nature Communications
volume
4
article number
1477
pages
1 - 8
publisher
Nature Publishing Group
external identifiers
  • pmid:23403578
  • scopus:84874584155
ISSN
2041-1723
DOI
10.1038/ncomms2470
language
English
LU publication?
no
additional info
Copyright: Copyright 2013 Elsevier B.V., All rights reserved.
id
7133880c-cd5a-48fc-9b10-d2d62694aa4b
date added to LUP
2021-09-24 20:48:21
date last changed
2025-07-29 19:26:13
@article{7133880c-cd5a-48fc-9b10-d2d62694aa4b,
  abstract     = {{<p>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.</p>}},
  author       = {{Li, Wen and Atkinson, Gemma C. and Thakor, Nehal S. and Allas, Ular and Lu, Chuao Chao and Yan Chan, Kwok and Tenson, Tanel and Schulten, Klaus and Wilson, Kevin S. and Hauryliuk, Vasili and Frank, Joachim}},
  issn         = {{2041-1723}},
  language     = {{eng}},
  pages        = {{1--8}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Nature Communications}},
  title        = {{Mechanism of tetracycline resistance by ribosomal protection protein Tet(O)}},
  url          = {{http://dx.doi.org/10.1038/ncomms2470}},
  doi          = {{10.1038/ncomms2470}},
  volume       = {{4}},
  year         = {{2013}},
}