Wen Li / Gemma C Atkinson / Nehal S Thakor / Ular Allas / Chuao-chao Lu / Kwok-Yan Chan / Tanel Tenson / Klaus Schulten / Kevin S Wilson / Vasili Hauryliuk / Joachim Frank /
PubMed 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 ...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.
EMDB-5562: tetracycline resistance protein Tet(O) bound to the ribosome PDB-4v6v: Tetracycline resistance protein Tet(O) bound to the ribosome Method: EM (single particle) / Resolution: 9.8 Å
Source
escherichia coli (E. coli)
campylobacter jejuni (Campylobacter)
Keywords
RIBOSOME / 70S ribosome / antibiotic resistance
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