ArticleThe Journal of biological chemistry2010
Uncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter.
Article in The Journal of biological chemistry, 2010. 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, 26 citations in OpenAlex.
- Structures of ABC transporters: handle with care.FEBS letters · 2020Review
- Structural basis of trehalose recycling by the ABC transporter LpqY-SugABC.Science advances · 2020Article
- Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein.Biochemistry · 2018Article
- Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter.Molecular microbiology · 2015Article
- Structural basis for substrate specificity in the Escherichia coli maltose transport system.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Molecular mechanism of the Escherichia coli maltose transporter.Current opinion in structural biology · 2013Review
- Substrate transport activation is mediated through second periplasmic loop of transmembrane protein MalF in maltose transport complex of Escherichia coli.The Journal of biological chemistry · 2012Article
- Tyrosine Phosphorylation of the BRI1 Receptor Kinase Occurs via a Post-Translational Modification and is Activated by the Juxtamembrane Domain.Frontiers in plant science · 2012Article
- Evidence for an allosteric mechanism of substrate release from membrane-transporter accessory binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- An integrated transport mechanism of the maltose ABC importer.Research in microbiologyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Members of the ATP-binding cassette superfamily couple the energy from ATP hydrolysis to the active transport of substrates across the membrane. The maltose transporter, a well characterized model system, consists of a periplasmic maltose-binding protein (MBP) and a multisubunit membrane transporter, MalFGK(2). On the basis of the structure of the MBP-MalFGK(2) complex in an outward-facing conformation (Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L., and Chen, J. (2007) Nature 450, 515-521), we identified two mutants in transmembrane domains MalF and MalG that generated futile cycling; although interaction with MBP stimulated the ATPase activity of the transporter, maltose was not transported. Both mutants appeared to disrupt the normal transfer of maltose from MBP to MalFGK(2). In the first case, substitution of aspartate for glycine in the maltose-binding site of MalF likely generated a futile cycle by preventing maltose from binding to MalFGK(2) during the catalytic cycle. In the second case, a four-residue deletion of a periplasmic loop of MalG limited its reach into the maltose-binding pocket of MBP, allowing maltose to remain associated with MBP during the catalytic cycle. Retention of maltose in the MBP binding site in the deletion mutant, as well as insertion of this loop into the binding site in the wild type, was detected by EPR as a change in mobility of a nitroxide spin label positioned near the maltose-binding pocket of MBP.
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