ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Local and Global Breathing Motions Prime the Access to Buried Binding Site in an Antibiotic-Sequestering Protein.ACS bio & med chem Au · 2025Article
- Convergent evolution of antibiotic resistance mechanisms between pyrrolobenzodiazepines and albicidin in multidrug resistant Klebsiella pneumoniae.npj antimicrobials and resistance · 2025Article
- IDRdecoder: a machine learning approach for rational drug discovery toward intrinsically disordered regions.Frontiers in bioinformatics · 2025Article
- A finely balanced order-disorder equilibrium sculpts the folding-binding landscape of an antibiotic sequestering protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Development of a thiostrepton-free system for stable production of PLD in Streptomyces lividans SBT5.Microbial cell factories · 2022Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Hinge region mediates signal transmission of luteinizing hormone and chorionic gonadotropin receptor.Computational and structural biotechnology journal · 2022Article
- Posttranslational chemical installation of azoles into translated peptides.Nature communications · 2021Article
- Antibiotic binding releases autoinhibition of the TipA multidrug-resistance transcriptional regulator.The Journal of biological chemistry · 2020Article
- Molecular insights into antibiotic resistance - how a binding protein traps albicidin.Nature communications · 2018Article
- YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.Chemical reviews · 2017Review
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Authors and funding
6 authors.
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Abstract
TipA is a transcriptional regulator found in diverse bacteria. It constitutes a minimal autoregulated multidrug resistance system against numerous thiopeptide antibiotics. Here we report the structures of its drug-binding domain TipAS in complexes with promothiocin A and nosiheptide, and a model of the thiostrepton complex. Drug binding induces a large transition from a partially unfolded to a globin-like structure. The structures rationalize the mechanism of promiscuous, yet specific, drug recognition: (i) a four-ring motif present in all known TipA-inducing antibiotics is recognized specifically by conserved TipAS amino acids; and (ii) the variable part of the antibiotic is accommodated within a flexible cleft that rigidifies upon drug binding. Remarkably, the identified four-ring motif is also the major interacting part of the antibiotic with the ribosome. Hence the TipA multidrug resistance mechanism is directed against the same chemical motif that inhibits protein synthesis. The observed identity of chemical motifs responsible for antibiotic function and resistance may be a general principle and could help to better define new leads for antibiotics.
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