ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structure of a pantothenate transporter and implications for ECF module sharing and energy coupling of group II ECF transporters.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 45 citations in OpenAlex.
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- Coenzyme A metabolism: a key driver of gut microbiota dynamics and metabolic profiles.FEMS microbiology reviews · 2025Review
- Identification of a depupylation regulator for an essential enzyme inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Expression and characterization of pantothenate energy-coupling factor transporters as an anti-infective drug target.Protein science : a publication of the Protein Society · 2024Article
- The S-component fold: a link between bacterial transporters and receptors.Communications biology · 2024Article
- 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
- Article
- Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology.International journal of molecular sciences · 2022Article
- Structure-Guided Optimization of Small-Molecule Folate Uptake Inhibitors Targeting the Energy-Coupling Factor Transporters.Journal of medicinal chemistry · 2022Article
- ATP-Binding Cassette Transporters: Snap-on Complexes?Sub-cellular biochemistry · 2022Article
- Insights into the bilayer-mediated toppling mechanism of a folate-specific ECF transporter by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Characterization of the Streptococcus mutansJournal of bacteriology · 2020Article
- Heme Uptake inApplied and environmental microbiology · 2020Article
- Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020Review
- Article
- Membrane mediated toppling mechanism of the folate energy coupling factor transporter.Nature communications · 2020Article
- Functional and structural characterization of an ECF-type ABC transporter for vitamin B12.eLife · 2018Article
- Structure and mechanism of a group-I cobalt energy coupling factor transporter.Cell research · 2017Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Energy-coupling factor (ECF) transporters are a unique group of ATP-binding cassette (ABC) transporters responsible for micronutrient uptake from the environment. Each ECF transporter is composed of an S component (or EcfS protein) and T/A/A' components (or EcfT/A/A' proteins; ECF module). Among the group II ECF transporters, several EcfS proteins share one ECF module; however, the underlying mechanism remains unknown. Here we report the structure of a group II ECF transporter-pantothenate transporter from Lactobacillus brevis (LbECF-PanT), which shares the ECF module with the folate and hydroxymethylpyrimidine transporters (LbECF-FolT and LbECF-HmpT). Structural and mutational analyses revealed the residues constituting the pantothenate-binding pocket. We found that although the three EcfS proteins PanT, FolT, and HmpT are dissimilar in sequence, they share a common surface area composed of the transmembrane helices 1/2/6 (SM1/2/6) to interact with the coupling helices 2/3 (CH2/3) of the same EcfT. CH2 interacts mainly with SM1 via hydrophobic interactions, which may modulate the sliding movement of EcfS. CH3 binds to a hydrophobic surface groove formed by SM1, SM2, and SM6, which may transmit the conformational changes from EcfA/A' to EcfS. We also found that the residues at the intermolecular surfaces in LbECF-PanT are essential for transporter activity, and that these residues may mediate intermolecular conformational transmission and/or affect transporter complex stability. In addition, we found that the structure of EcfT is conformationally dynamic, which supports its function as a scaffold to mediate the interaction of the ECF module with various EcfS proteins to form different transporter complexes.
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