ArticleThe Journal of biological chemistry2015
Salt Bridge Swapping in the EXXERFXYY Motif of Proton-coupled Oligopeptide Transporters.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 41 citations in OpenAlex.
- Defined roles for the Staphylococcus aureus POT transporter DtpT in di/tripeptide uptake and glutathione utilisation inside human macrophages.PLoS pathogens · 2025Article
- Structural basis for antibiotic transport and inhibition in PepT2.Nature communications · 2024Article
- Article
- Structural basis for antibiotic transport and inhibition in PepT2, the mammalian proton-coupled peptide transporter.Research square · 2024Article
- Functional Characterization of the Putative POT fromBiology · 2023Article
- Structural Insights into the Substrate Transport Mechanisms in GTR Transporters through Ensemble Docking.International journal of molecular sciences · 2022Article
- Genome- and transcriptome-wide association studies reveal the genetic basis and the breeding history of seed glucosinolate content in Brassica napus.Plant biotechnology journal · 2022Article
- Cryo-EM Structure of an Atypical Proton-Coupled Peptide Transporter: Di- and Tripeptide Permease C.Frontiers in molecular biosciences · 2022Article
- Cryo-EM structure of PepT2 reveals structural basis for proton-coupled peptide and prodrug transport in mammals.Science advances · 2021Article
- Structural Modeling andFrontiers in plant science · 2021Article
- Recent advances in understanding prodrug transport through the SLC15 family of proton-coupled transporters.Biochemical Society transactions · 2020Review
- Structural basis for prodrug recognition by the SLC15 family of proton-coupled peptide transporters.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- An Optimized Screen Reduces the Number of GA Transporters and Provides Insights Into Nitrate Transporter 1/Peptide Transporter Family Substrate Determinants.Frontiers in plant science · 2019Article
- The prototypical proton-coupled oligopeptide transporter YdgR fromThe Journal of biological chemistry · 2018Article
- Recent advances in understanding proton coupled peptide transport via the POT family.Current opinion in structural biology · 2017Review
- Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Proton-coupled oligopeptide transporters (POTs) couple the inward transport of di- or tripeptides with an inwardly directed transport of protons. Evidence from several studies of different POTs has pointed toward involvement of a highly conserved sequence motif, E1XXE2RFXYY (from here on referred to as E1XXE2R), located on Helix I, in interactions with the proton. In this study, we investigated the intracellular substrate accumulation by motif variants with all possible combinations of glutamate residues changed to glutamine and arginine changed to a tyrosine, the latter being a natural variant found in the Escherichia coli POT YjdL. We found that YjdL motif variants with E1XXE2R, E1XXE2Y, E1XXQ2Y, or Q1XXE2Y were able to accumulate peptide, whereas those with E1XXQ2R, Q1XXE2R, or Q1XXQ2Y were unable to accumulate peptide, and Q1XXQ2R abolished uptake. These results suggest a mechanism that involves swapping of an intramotif salt bridge, i.e. R-E2 to R-E1, which is consistent with previous structural studies. Molecular dynamics simulations of the motif variants E1XXE2R and E1XXQ2R support this mechanism. The simulations showed that upon changing conformation arginine pushes Helix V, through interactions with the highly conserved FYING motif, further away from the central cavity in what could be a stabilization of an inward facing conformation. As E2 has been suggested to be the primary site for protonation, these novel findings show how protonation may drive conformational changes through interactions of two highly conserved motifs.
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