ArticleMolecular microbiology2015
Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Developing hybrid thiomaltodextrins as specific ligands to the maltodextrin transporter ofRSC advances · 2026Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- Synthesis, radiolabeling, and biological evaluation of methyl 6-deoxy-6-[RSC advances · 2025Article
- Mechanistic Investigation of the Pyrolysis Temperature of Reed Wood Vinegar for Maximising the Antibacterial Activity ofBiology · 2024Article
- Functional Overexpression of Membrane Proteins in E. coli: The Good, the Bad, and the Ugly.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Functional integrity of membrane protein rhodopsin solubilized by styrene-maleic acid copolymer.Biophysical journal · 2021Article
- ATP hydrolysis and nucleotide exit enhance maltose translocation in the MalFGKScientific reports · 2021Article
- Molecular Characterization of the Extracellular Domain of Human Junctional Adhesion Proteins.International journal of molecular sciences · 2021Article
- Structures of ABC transporters: handle with care.FEBS letters · 2020Review
- DirectMX - One-Step Reconstitution of Membrane Proteins From Crude Cell Membranes Into Salipro Nanoparticles.Frontiers in bioengineering and biotechnology · 2020Article
- Functionality of membrane proteins overexpressed and purified from E. coli is highly dependent upon the strain.Scientific reports · 2019Article
- Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA fromCommunications biology · 2019Article
- Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein.Biochemistry · 2018Article
- A multidrug ABC transporter with a taste for GTP.Scientific reports · 2018Article
- Gradient reconstitution of membrane proteins for solid-state NMR studies.Journal of biomolecular NMR · 2017Article
- Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalKThe Journal of biological chemistry · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Nanodiscs for structural and functional studies of membrane proteins.Nature structural & molecular biology · 2016Review
- An integrated transport mechanism of the maltose ABC importer.Research in microbiologyReview
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
MalFGK2 is an ATP-binding cassette (ABC) transporter that mediates the uptake of maltose/maltodextrins into Escherichia coli. A periplasmic maltose-binding protein (MBP) delivers maltose to the transmembrane subunits (MalFG) and stimulates the ATPase activity of the cytoplasmic nucleotide-binding subunits (MalK dimer). This MBP-stimulated ATPase activity is independent of maltose for purified transporter in detergent micelles. However, when the transporter is reconstituted in membrane bilayers, only the liganded form of MBP efficiently stimulates its activity. To investigate the mechanism of maltose stimulation, electron paramagnetic resonance spectroscopy was used to study the interactions between the transporter and MBP in nanodiscs and in detergent. We found that full engagement of both lobes of maltose-bound MBP unto MalFGK2 is facilitated by nucleotides and stabilizes a semi-open MalK dimer. Maltose-bound MBP promotes the transition to the semi-open state of MalK when the transporter is in the membrane, whereas such regulation does not require maltose in detergent. We suggest that stabilization of the semi-open MalK2 conformation by maltose-bound MBP is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP.
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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.