ArticleOpen biology2021
Structural and biophysical characterization of the tandem substrate-binding domains of the ABC importer GlnPQ.
Article in Open biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Dissecting mechanisms of ligand binding and conformational changes in the glutamine-binding protein.eLife · 2026Article
- Single-Molecule Forster Resonance Energy Transfer With a Minimalistic 3D-Printed Setup and Dyes in the Blue-Green Spectral Region.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- Exploring the Ligand Binding and Conformational Dynamics of the Substrate-Binding Domain 1 of the ABC Transporter GlnPQ.The journal of physical chemistry. B · 2024Article
- How arginine inhibits substrate-binding domain 2 elucidated using molecular dynamics simulations.Protein science : a publication of the Protein Society · 2024Article
- A new twist on PIFE: photoisomerisation-related fluorescence enhancement.Methods and applications in fluorescence · 2023Review
- Article
- Biophysical Approaches for the Characterization of Protein-Metabolite Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Review
- Structural and biophysical characterization of the tandem substrate-binding domains of the ABC importer GlnPQ.Open biology · 2021Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ATP-binding cassette transporter GlnPQ is an essential uptake system that transports glutamine, glutamic acid and asparagine in Gram-positive bacteria. It features two extra-cytoplasmic substrate-binding domains (SBDs) that are linked in tandem to the transmembrane domain of the transporter. The two SBDs differ in their ligand specificities, binding affinities and their distance to the transmembrane domain. Here, we elucidate the effects of the tandem arrangement of the domains on the biochemical, biophysical and structural properties of the protein. For this, we determined the crystal structure of the ligand-free tandem SBD1-2 protein from
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Registered trials
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.