ArticleCell chemical biology2016
Crystal Structure of a Group I Energy Coupling Factor Vitamin Transporter S Component in Complex with Its Cognate Substrate.
Article in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Increased Availability of Selective Trace Elements Enhanced Anaerobic Benzoate Oxidation inMicroorganisms · 2026Article
- Genomic Characterization of MarineMicroorganisms · 2025Article
- Vitamin biosynthesis in the gut: interplay between mammalian host and its resident microbiota.Microbiology and molecular biology reviews : MMBR · 2025Review
- Comparative Genomic and Genetic Evidence on a Role for the OarX Protein in Thiamin Salvage.ACS omega · 2024Article
- Characterization of the Streptococcus mutansJournal of bacteriology · 2020Article
- Article
- The Iron Deficiency Response of Corynebacterium glutamicum and a Link to Thiamine Biosynthesis.Applied and environmental microbiology · 2020Article
- Membrane mediated toppling mechanism of the folate energy coupling factor transporter.Nature communications · 2020Article
- Lipid-like Peptides can Stabilize Integral Membrane Proteins for Biophysical and Structural Studies.Chembiochem : a European journal of chemical biology · 2017Article
- A Novel Transcriptional Regulator Related to Thiamine Phosphate Synthase Controls Thiamine Metabolism Genes in Archaea.Journal of bacteriology · 2017Article
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Authors and funding
4 authors.
Funding
Abstract
Energy coupling factor (ECF) transporters are responsible for the uptake of essential scarce nutrients in prokaryotes. This ATP-binding cassette transporter family comprises two subgroups that share a common architecture forming a tripartite membrane protein complex consisting of a translocation component and ATP hydrolyzing module and a substrate-capture (S) component. Here, we present the crystal structure of YkoE from Bacillus subtilis, the S component of the previously uncharacterized group I ECF transporter YkoEDC. Structural and biochemical analyses revealed the constituent residues of the thiamine-binding pocket as well as an unexpected mode of vitamin recognition. In addition, our experimental and bioinformatics data demonstrate major differences between YkoE and group II ECF transporters and indicate how group I vitamin transporter S components have diverged from other group I and group II ECF transporters.
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