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

Proc. Natl. Acad. Sci. U.S.A.2013 Mar 05;110(10):3812-6. Epub 2013 Feb 19

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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.

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

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