ArticleProceedings of the National Academy of Sciences of the United States of America2013
Assembly and mechanism of a group II ECF transporter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Increased Availability of Selective Trace Elements Enhanced Anaerobic Benzoate Oxidation inMicroorganisms · 2026Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- Identification of inhibitors targeting the energy-coupling factor (ECF) transporters.Communications biology · 2023Article
- Expulsion mechanism of the substrate-translocating subunit in ECF transporters.Nature communications · 2023Article
- ATP-Binding Cassette Transporters: Snap-on Complexes?Sub-cellular biochemistry · 2022Article
- Characterization of the Streptococcus mutansJournal of bacteriology · 2020Article
- Be Cautious with Crystal Structures of Membrane Proteins or Complexes Prepared in Detergents.Crystals · 2020Article
- Predicting the optimal growth temperatures of prokaryotes using only genome derived features.Bioinformatics (Oxford, England) · 2019Article
- The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair.Nucleic acids research · 2019Article
- A Novel Prokaryote-Type ECF/ABC Transporter Module in Chloroplast Metal Homeostasis.Frontiers in plant science · 2019Article
- Uptake and Metabolism of Antibiotics Roseoflavin and 8-Demethyl-8-Aminoriboflavin in Riboflavin-Auxotrophic Listeria monocytogenes.Journal of bacteriology · 2016Article
- An Aromatic Cap Seals the Substrate Binding Site in an ECF-Type S Subunit for Riboflavin.Journal of molecular biology · 2016Article
- ATP-dependent Conformational Changes Trigger Substrate Capture and Release by an ECF-type Biotin Transporter.The Journal of biological chemistry · 2015Article
- ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism.Nature structural & molecular biology · 2015Article
- Pyridoxamine is a substrate of the energy-coupling factor transporter HmpT.Cell discovery · 2015Article
- Complete Genome Sequence of Thermus aquaticus Y51MC23.PloS one · 2015Article
- Structure of a pantothenate transporter and implications for ECF module sharing and energy coupling of group II ECF transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters.Cell research · 2014Article
- Structural and mechanistic insights into prokaryotic energy-coupling factor transporters.Nature reviews. Microbiology · 2014Article
- Structural basis for a homodimeric ATPase subunit of an ECF transporter.Protein & cell · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Energy-coupling factor (ECF) transporters are a recently discovered family of primary active transporters for micronutrients and vitamins, such as biotin, thiamine, and riboflavin. Found exclusively in archaea and bacteria, including the human pathogens Listeria, Streptococcus, and Staphylococcus, ECF transporters may be the only means of vitamin acquisition in these organisms. The subunit composition of ECF transporters is similar to that of ATP binding cassette (ABC) importers, whereby both systems share two homologous ATPase subunits (A and A'), a high affinity substrate-binding subunit (S), and a transmembrane coupling subunit (T). However, the S subunit of ECF transporters is an integral membrane protein, and the transmembrane coupling subunits do not share an obvious sequence homology between the two transporter families. Moreover, the subunit stoichiometry of ECF transporters is controversial, and the detailed molecular interactions between subunits and the conformational changes during substrate translocation are unknown. We have characterized the ECF transporters from Thermotoga maritima and Streptococcus thermophilus. Our data suggests a subunit stoichiometry of 2S:2T:1A:1A' and that S subunits for different substrates can be incorporated into the same transporter complex simultaneously. In the first crystal structure of the A-A' heterodimer, each subunit contains a novel motif called the Q-helix that plays a key role in subunit coupling with the T subunits. Taken together, these findings suggest a mechanism for coupling ATP binding and hydrolysis to transmembrane transport by ECF transporters.
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