ArticleJournal of bacteriology2009
The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Developing hybrid thiomaltodextrins as specific ligands to the maltodextrin transporter ofRSC advances · 2026Article
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- Ligand-binding properties of substrate binding proteins of a maltose uptake system inMicrobiology (Reading, England) · 2026Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- G-quadruplex stabilization in the ions and maltose transporters gene inhibit Salmonella enterica growth and virulence.Genomics · 2020Article
- Formation of a Chloride-conducting State in the Maltose ATP-binding Cassette (ABC) Transporter.The Journal of biological chemistry · 2016Article
- Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter.Molecular microbiology · 2015Article
- Structure determination of a sugar-binding protein from the phytopathogenic bacterium Xanthomonas citri.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Role of the two structural domains from the periplasmic Escherichia coli histidine-binding protein HisJ.The Journal of biological chemistry · 2013Article
- Conformational plasticity of the type I maltose ABC importer.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Enterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose 6'-phosphate phosphatase (MapP).Molecular microbiology · 2013Article
- Article
- Inter-domain communication mechanisms in an ABC importer: a molecular dynamics study of the MalFGK2E complex.PLoS computational biology · 2011Article
- Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate.The Journal of biological chemistry · 2010Article
- The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds.Molecular microbiology · 2010Article
- Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer.The Journal of biological chemistry · 2009Article
- An integrated transport mechanism of the maltose ABC importer.Research in microbiologyReview
- Diversity in ABC transporters: type I, II and III importers.Critical reviews in biochemistry and molecular biologyReview
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have investigated the interaction of the uncommonly large periplasmic P2 loop of the MalF subunit of the maltose ATP-binding cassette transporter (MalFGK(2)) from Escherichia coli and Salmonella enterica serovar Typhimurium with maltose binding protein (MalE) by site-specific chemical cross-linking in the assembled transport complex. We focused on possible distance changes between two pairs of residues of the P2 loop and MalE during the transport cycle. The distance between MalF(S205C) and MalE(T80C) ( approximately 5 A) remained unchanged under all conditions tested. Cross-linking did not affect the ATPase activity of the complex. The distance between MalF(T177C) and MalE(T31C) changed from approximately 10 A to approximately 5 A upon binding of ATP (or maltose, with a less pronounced result) and was reset to approximately 10 A after hydrolysis of one ATP. A cross-link ( approximately 25 A) between MalF(S205C) and MalE(T31C) was observed only when the transporter resided in a transition state-like conformation, as was the case after vanadate trapping or in a binding protein-independent mutant, both of which are characterized by tight binding of unliganded MalE to the transporter. Thus, we propose that the observed cross-link is indicative of catalytic intermediates of the transporter. Together, our results strengthen the notion that the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. The data are discussed with respect to a crystal structure and current transport models.
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