ArticleNature communications2015
Structures of FolT in substrate-bound and substrate-released conformations reveal a gating mechanism for ECF transporters.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Impact of Host and Bacterial Metabolism on Antibiotic Susceptibility.Biochemistry · 2025Review
- Assembly and Analysis of Cell-Scale Membrane Envelopes.Journal of chemical information and modeling · 2022Article
- Article
- Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020Review
- Membrane mediated toppling mechanism of the folate energy coupling factor transporter.Nature communications · 2020Article
- The uridylyltransferase GlnD and tRNA modification GTPase MnmE allosterically controlThe Journal of biological chemistry · 2018Article
- A defensin-like protein drives cadmium efflux and allocation in rice.Nature communications · 2018Article
- Structure and mechanism of a group-I cobalt energy coupling factor transporter.Cell research · 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
- Structural insight in the toppling mechanism of an energy-coupling factor transporter.Nature communications · 2016Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Energy-coupling factor (ECF) transporters are a new family of ABC transporters that consist of four subunits, two cytoplasmic ATPases EcfA and EcfA' and two transmembrane proteins namely EcfS for substrate-specific binding and EcfT for energy coupling. Here, we report the 3.2-Å resolution crystal structure of the EcfS protein of a folate ECF transporter from Enterococcus faecalis-EfFolT, a close homologue of FolT from Lactobacillus brevis-LbFolT. Structural and biochemical analyses reveal the residues constituting the folate-binding pocket and determining the substrate-binding specificity. Structural comparison of the folate-bound EfFolT with the folate-free LbFolT contained in the holotransporter complex discloses significant conformational change at the L1 loop, and reveals a gating mechanism of ECF transporters in which the L1 loop of EcfS acts as a gate in the substrate binding and release.
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