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

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

Proceedings of the National Academy of Sciences of the United States of America (2013-02-23)
Lasse Jenner, Agata L Starosta, Daniel S Terry, Aleksandra Mikolajka, Liudmila Filonava, Marat Yusupov, Scott C Blanchard, Daniel N Wilson, Gulnara Yusupova
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Gly-Gly, BioPerformance Certified, suitable for cell culture, ≥99%
Sigma-Aldrich
Gly-Gly, BioUltra, ≥99.5% (NT)
Sigma-Aldrich
Gly-Gly, ≥99% (titration)