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Proc Natl Acad Sci U S A. 2013 Mar 5;110(10):3812-6. doi: 10.1073/pnas.1216691110. Epub 2013 Feb 19.

Structural basis for potent inhibitory activity of the antibiotic tigecycline during protein synthesis.

Author information

1
Institut National de la Santé et de la Recherche Médicale U964, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 7104, 67404 Illkirch, France.

Abstract

Here we present an X-ray crystallography structure of the clinically relevant tigecycline antibiotic bound to the 70S ribosome. Our structural and biochemical analysis indicate that the enhanced potency of tigecycline results from a stacking interaction with nucleobase C1054 within the decoding site of the ribosome. Single-molecule fluorescence resonance energy transfer studies reveal that, during decoding, tigecycline inhibits the initial codon recognition step of tRNA accommodation and prevents rescue by the tetracycline-resistance protein TetM.

PMID:
23431179
PMCID:
PMC3593886
DOI:
10.1073/pnas.1216691110
[Indexed for MEDLINE]
Free PMC Article

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