ArticleScientific reports2014
Dynamic multidrug recognition by multidrug transcriptional repressor LmrR.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 56 citations in OpenAlex.
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- Exploring PadR Proteins for Artificial Enzyme Design.Chembiochem : a European journal of chemical biology · 2026Article
- Activity-Enhancing Mutations in an LmrR-Based Artificial Metalloenzyme Destabilize the Protein Scaffold and Alter its Conformational Plasticity.Chembiochem : a European journal of chemical biology · 2025Article
- Evolutionary Specialization of a Promiscuous Designer Enzyme.ACS catalysis · 2025Article
- Rationally introducing non-canonical amino acids to enhance catalytic activity of LmrR for Henry reaction.Bioresources and bioprocessing · 2024Article
- The Role of Tryptophan in π Interactions in Proteins: An Experimental Approach.Journal of the American Chemical Society · 2022Article
- A Versatile Transcription Factor Biosensor System Responsive to Multiple Aromatic and Indole Inducers.ACS synthetic biology · 2022Article
- Chemogenetic Tags with Probe Exchange for Live-Cell Fluorescence Microscopy.ACS chemical biology · 2021Article
- Elements in the LftR Repressor Operator Interface Contributing to Regulation of Aurantimycin Resistance in Listeria monocytogenes.Journal of bacteriology · 2021Article
- In Vivo Assembly of Artificial Metalloenzymes and Application in Whole-Cell Biocatalysis*.Angewandte Chemie (International ed. in English) · 2021Article
- High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin.Magnetic resonance (Gottingen, Germany) · 2021Article
- The role of NMR in leveraging dynamics and entropy in drug design.Journal of biomolecular NMR · 2020Article
- Cofactor Binding Dynamics Influence the Catalytic Activity and Selectivity of an Artificial Metalloenzyme.ACS catalysis · 2020Article
- Targeting the cryptic sites: NMR-based strategy to improve protein druggability by controlling the conformational equilibrium.Science advances · 2020Article
- Artificial Metalloenzymes based on TetR Proteins and Cu(II) for Enantioselective Friedel-Crafts Alkylation Reactions.ChemCatChem · 2020Article
- Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR.International journal of molecular sciences · 2020Review
- Conformational equilibrium defines the variable induction of the multidrug-binding transcriptional repressor QacR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- PadR-type repressors controlling production of a non-canonical FtsW/RodA homologue and other trans-membrane proteins.Scientific reports · 2019Article
- LmrR: A Privileged Scaffold for Artificial Metalloenzymes.Accounts of chemical research · 2019Article
- Characterization of Internal Protein Dynamics and Conformational Entropy by NMR Relaxation.Methods in enzymology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LmrR is a multidrug transcriptional repressor that controls the expression of a major multidrug transporter, LmrCD, in Lactococcus lactis. However, the molecular mechanism by which LmrR binds to structurally unrelated compounds and is released from the promoter region remains largely unknown. Here, we structurally and dynamically characterized LmrR in the apo, compound-bound and promoter-bound states. The compound-binding site of LmrR exhibits ps-μs dynamics in the apo state, and compound ligation shifts the preexisting conformational equilibrium to varying extents to achieve multidrug recognition. Meanwhile, the compound binding induces redistribution of ps-ns dynamics to the allosteric sites, which entropically favors the high-affinity recognition. Furthermore, the reciprocal compound/promoter binding by LmrR is achieved by the incompatible conformational ensembles between the compound- and promoter-bound states. Collectively, the data show how LmrR can dynamically exert its functions through promiscuous multi-target interactions, in a manner that cannot be understood by a static structural view.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.