Structural basis for potent inhibitory activity of the antibiotic tigecycline during protein synthesis Academic Article uri icon

Overview

MeSH Major

  • Anti-Bacterial Agents
  • Minocycline

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.

publication date

  • March 5, 2013

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3593886

Digital Object Identifier (DOI)

  • 10.1073/pnas.1216691110

PubMed ID

  • 23431179

Additional Document Info

start page

  • 3812

end page

  • 6

volume

  • 110

number

  • 10