ArticleBiochemistry2010
Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 62 citations in OpenAlex.
- Real-time simultaneous monitoring of multiple analytes in bacterial cultures.Applied and environmental microbiology · 2025Article
- Evaluating the use of lanthanide containing dendrimers for solvent paramagnetic relaxation enhancement.Journal of biomolecular NMR · 2025Article
- Discovery of periplasmic solute binding proteins with specificity for ketone bodies: β-hydroxybutyrate binding proteins.Protein science : a publication of the Protein Society · 2024Article
- Structural and bioinformatics analysis of single-domain substrate-binding protein fromBiochemistry and biophysics reports · 2024Article
- Retracing the evolution of a modern periplasmic binding protein.Protein science : a publication of the Protein Society · 2023Article
- Revealing Allosteric Mechanism of Amino Acid Binding Proteins from Open to Closed State.Molecules (Basel, Switzerland) · 2023Article
- Engineering a Conformationally Switchable Artificial Metalloprotein.Journal of the American Chemical Society · 2022Article
- Article
- Structural basis for a bacterial Pip system plant effector recognition protein.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Simultaneous measurement ofJournal of biomolecular NMR · 2021Article
- Ligand binding and global adaptation of the GlnPQ substrate binding domain 2 revealed by molecular dynamics simulations.Protein science : a publication of the Protein Society · 2020Article
- Ligand-bound glutamine binding protein assumes multiple metastable binding sites with different binding affinities.Communications biology · 2020Article
- NMR Analysis of Apo Glutamine-Binding Protein Exposes Challenges in the Study of Interdomain Dynamics.Angewandte Chemie (International ed. in English) · 2019Article
- Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein.Nature chemical biology · 2018Article
- Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein.International journal of molecular sciences · 2017Article
- PELDOR Spectroscopy Reveals Two Defined States of a Sialic Acid TRAP Transporter SBP in Solution.Biophysical journal · 2017Article
- Molecular lock regulates binding of glycine to a primitive NMDA receptor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa.Structure (London, England : 1993) · 2016Article
- Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags.Journal of biomolecular NMR · 2016Article
- Conformational dynamics in substrate-binding domains influences transport in the ABC importer GlnPQ.Nature structural & molecular biology · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The ability to undergo large-scale domain rearrangements is essential for the substrate-binding function of periplasmic binding proteins (PBPs), which are indispensable for nutrient uptake in Gram-negative bacteria. Crystal structures indicate that PBPs typically adopt either an "open" unliganded configuration or a "closed" liganded one. However, it is not clear whether, as a general rule, PBPs remain open until ligand-induced interdomain closure or are in equilibrium with a minor population of unliganded, closed species. Evidence for the latter has been recently reported on maltose-binding protein (MBP) in aqueous solution [Tang, C., et al. (2007) Nature 449, 1078-1082] via paramagnetic relaxation enhancement (PRE), a technique able to probe lowly populated regions of conformational space. Here, we use PRE to study the unliganded open-closed transition of another PBP: glutamine-binding protein (GlnBP). Through a combination of domain structure knowledge and intermolecular and concentration dependence PRE experiments, a set of surface residues was found to be involved in intermolecular interactions. Barring such residues, PRE data on ligand-free GlnBP, paramagnetically labeled at two sites (one at a time), could be appropriately explained by the unliganded, open crystal structure in that it both yielded a good PRE fit and was not significantly affected by PRE-based refinement. Thus, contrary to MBP, our data did not particularly suggest the coexistence of a minor closed conformer. Several possibilities were explored to explain the observed differences in such closely structurally related systems; among them, a particularly interesting one arises from close inspection of the interdomain "hinge" region of various PBPs: strong hydrogen bond interactions discourage large-scale interdomain dynamics.
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