ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural divergence of paralogous S components from ECF-type ABC transporters.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 63 citations in OpenAlex.
- Biotin synthesis and assimilation are vital for pathobiology of the insect pathogenic fungusMycology · 2026Article
- The S-component fold: a link between bacterial transporters and receptors.Communications biology · 2024Article
- Lactiplantibacillus plantarum as a novel platform for production and purification of integral membrane proteins using RseP as the benchmark.Scientific reports · 2023Article
- Expulsion mechanism of the substrate-translocating subunit in ECF transporters.Nature communications · 2023Article
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- Review
- 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
- 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
- Be Cautious with Crystal Structures of Membrane Proteins or Complexes Prepared in Detergents.Crystals · 2020Article
- Cysteine-mediated decyanation of vitamin B12 by the predicted membrane transporter BtuM.Nature communications · 2018Article
- 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
- Targeted Diazotransfer Reagents Enable Selective Modification of Proteins with Azides.Bioconjugate chemistry · 2017Article
- An Aromatic Cap Seals the Substrate Binding Site in an ECF-Type S Subunit for Riboflavin.Journal of molecular biology · 2016Article
- Crystal Structure of a Group I Energy Coupling Factor Vitamin Transporter S Component in Complex with Its Cognate Substrate.Cell chemical biology · 2016Article
- Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis.Scientific reports · 2016Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Energy coupling factor (ECF) proteins are ATP-binding cassette transporters involved in the import of micronutrients in prokaryotes. They consist of two nucleotide-binding subunits and the integral membrane subunit EcfT, which together form the ECF module and a second integral membrane subunit that captures the substrate (the S component). Different S components, unrelated in sequence and specific for different ligands, can interact with the same ECF module. Here, we present a high-resolution crystal structure at 2.1 Å of the biotin-specific S component BioY from Lactococcus lactis. BioY shares only 16% sequence identity with the thiamin-specific S component ThiT from the same organism, of which we recently solved a crystal structure. Consistent with the lack of sequence similarity, BioY and ThiT display large structural differences (rmsd = 5.1 Å), but the divergence is not equally distributed over the molecules: The S components contain a structurally conserved N-terminal domain that is involved in the interaction with the ECF module and a highly divergent C-terminal domain that binds the substrate. The domain structure explains how the S components with large overall structural differences can interact with the same ECF module while at the same time specifically bind very different substrates with subnanomolar affinity. Solitary BioY (in the absence of the ECF module) is monomeric in detergent solution and binds D-biotin with a high affinity but does not transport the substrate across the membrane.
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