ArticleCommunications biology2024
Probing the allosteric NBD-TMD crosstalk in the ABC transporter MsbA by solid-state NMR.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Breaking the outer membrane barrier: structure, targets, and antimicrobial strategies for Gram-negative bacteria.Frontiers in microbiology · 2026Review
- Bidirectional communication between nucleotide and substrate binding sites in a type IV multidrug ABC transporter.Nature communications · 2025Article
- Conformational Plasticity of LptC Regulates Lipopolysaccharide Transport by the LptBJournal of the American Chemical Society · 2025Article
- Lipopolysaccharide: Recent Advances in Its Biosynthesis and Controlling Cell Envelope Homeostasis.International journal of molecular sciences · 2025Article
- Rhodamine6G and Hœchst33342 narrow BmrA conformational spectrum for a more efficient use of ATP.Nature communications · 2025Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The ABC transporter MsbA plays a critical role in Gram-negative bacteria in the regulation of the outer membrane by translocating core-LPS across the inner membrane. Additionally, a broad substrate specificity for lipophilic drugs has been shown. The allosteric interplay between substrate binding in the transmembrane domains and ATP binding and turnover in the nucleotide-binding domains must be mediated via the NBD/TMD interface. Previous studies suggested the involvement of two intracellular loops called coupling helix 1 and 2 (CH1, CH2). Here, we demonstrate by solid-state NMR spectroscopy that substantial chemical shift changes within both CH1 and CH2 occur upon substrate binding, in the ATP hydrolysis transition state, and upon inhibitor binding. CH2 is domain-swapped within the MsbA structure, and it is noteworthy that substrate binding induces a larger response in CH2 compared to CH1. Our data demonstrate that CH1 and CH2 undergo structural changes as part of the TMD-NBD cross-talk.
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Registered trials
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