ArticleProceedings of the National Academy of Sciences of the United States of America2008
Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 103 citations in OpenAlex.
- Microbial membrane transport genes in maize rhizosphere under fertilization - a preliminary study.Scientific reports · 2026Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- How arginine inhibits substrate-binding domain 2 elucidated using molecular dynamics simulations.Protein science : a publication of the Protein Society · 2024Article
- Daptomycin avoids drug resistance mediated by the BceAB transporter inMicrobiology spectrum · 2024Article
- The transport activity of the multidrug ABC transporter BmrA does not require a wide separation of the nucleotide-binding domains.The Journal of biological chemistry · 2024Article
- Structures of ABC transporters: handle with care.FEBS letters · 2020Review
- Evidence from Mutational Analysis for a Single Transmembrane Substrate Binding Site in the Histidine ATP-Binding Cassette Transporter of Salmonella enterica Serovar Typhimurium.Journal of bacteriology · 2019Article
- One Intact Transmembrane Substrate Binding Site Is Sufficient for the Function of the Homodimeric Type I ATP-Binding Cassette Importer for Positively Charged Amino Acids Art(MP)Journal of bacteriology · 2018Article
- Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein.Biochemistry · 2018Article
- Engineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins.The Journal of biological chemistry · 2018Article
- Structure and mechanism of a group-I cobalt energy coupling factor transporter.Cell research · 2017Article
- Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalKThe Journal of biological chemistry · 2017Article
- Biochemical characterization of essential cell division proteins FtsX and FtsE that mediate peptidoglycan hydrolysis by PcsB in Streptococcus pneumoniae.MicrobiologyOpen · 2016Article
- Thermodynamics of ABC transporters.Protein & cell · 2016Review
- Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter.Molecular microbiology · 2015Article
- Sequential Action of MalE and Maltose Allows Coupling ATP Hydrolysis to Translocation in the MalFGK2 Transporter.The Journal of biological chemistry · 2015Article
- Article
- ATP-dependent Conformational Changes Trigger Substrate Capture and Release by an ECF-type Biotin Transporter.The Journal of biological chemistry · 2015Article
- Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment.The Journal of biological chemistry · 2014Article
- Nucleotide-free MalK drives the transition of the maltose transporter to the inward-facing conformation.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The maltose transporter MalFGK(2) of Escherichia coli is a member of the ATP-binding cassette superfamily. A periplasmic maltose-binding protein (MBP) delivers maltose to MalFGK(2) and stimulates its ATPase activity. Site-directed spin labeling EPR spectroscopy was used to study the opening and closing of the nucleotide-binding interface of MalFGK(2) during the catalytic cycle. In the intact transporter, closure of the interface coincides not just with the binding of ATP, as seen with isolated nucleotide-binding domains, but requires both MBP and ATP, implying that MBP stimulates ATPase activity by promoting the closure of the nucleotide-binding interface. After ATP hydrolysis, with MgADP and MBP bound, the nucleotide-binding interface resides in a semi-open configuration distinct from the fully open configuration seen in the absence of any ligand. We propose that P(i) release coincides with the reorientation of transmembrane helices to an inward-facing conformation and the final step of maltose translocation into the cell.
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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.