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• W2106528306 abstract "The polyketide natural product borrelidin displays antibacterial, antifungal, antimalarial, anticancer, insecticidal and herbicidal activities through the selective inhibition of threonyl-tRNA synthetase (ThrRS). How borrelidin simultaneously attenuates bacterial growth and suppresses a variety of infections in plants and animals is not known. Here we show, using X-ray crystal structures and functional analyses, that a single molecule of borrelidin simultaneously occupies four distinct subsites within the catalytic domain of bacterial and human ThrRSs. These include the three substrate-binding sites for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite created as a consequence of binding. Thus, borrelidin competes with all three aminoacylation substrates, providing a potent and redundant mechanism to inhibit ThrRS during protein synthesis. These results highlight a surprising natural design to achieve the quadrivalent inhibition of translation through a highly conserved family of enzymes." @default.
• W2106528306 created "2016-06-24" @default.
• W2106528306 creator A5003643547 @default.
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• W2106528306 date "2015-03-31" @default.
• W2106528306 modified "2023-10-12" @default.
• W2106528306 title "Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetase" @default.
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• W2106528306 doi "https://doi.org/10.1038/ncomms7402" @default.
• W2106528306 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4389257" @default.
• W2106528306 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25824639" @default.
• W2106528306 hasPublicationYear "2015" @default.
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