ArticleStructure (London, England : 1993)2015
Gating topology of the proton-coupled oligopeptide symporters.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
55 citing papers in PubMed, 129 citations in OpenAlex.
- Structural basis of glucosinolate recognition and polyspecific transport by the glucosinolate transporter GTR1.The Journal of biological chemistry · 2026Article
- Structural basis for prostaglandin and drug transport via SLCO2A1.Nature communications · 2026Article
- A model for drug transport across two membranes of Gram-negative bacteria by an MFS tripartite assembly.Nature communications · 2026Article
- Identification of New Key Players for Ferrous Iron Export in the Asymmetric Inner Gate of Human Ferroportin 1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Energetics of substrate transport in proton-dependent oligopeptide transporters.Communications chemistry · 2024Article
- The dual loss and gain of function of the FPN1 iron exporter results in the ferroportin disease phenotype.HGG advances · 2024Article
- Structural basis for antibiotic transport and inhibition in PepT2.Nature communications · 2024Article
- Article
- Molecular basis for selective uptake and elimination of organic anions in the kidney by OAT1.Nature structural & molecular biology · 2023Article
- Role of peptide transporters in small peptide uptake of bovine mammary epithelial cells cultured in a transwell chamber.Food science & nutrition · 2023Article
- Inhibition of Multidrug Efflux Pumps Belonging to the Major Facilitator Superfamily in Bacterial Pathogens.Biomedicines · 2023Review
- Functional Characterization of the Putative POT fromBiology · 2023Article
- Ins and Outs of Rocker Switch Mechanism in Major Facilitator Superfamily of Transporters.Membranes · 2023Review
- Biology of Peptide Transporter 2 in Mammals: New Insights into Its Function, Structure and Regulation.Cells · 2022Review
- General principles of secondary active transporter function.Biophysics reviews · 2022Review
- Peptide transporter structure reveals binding and action mechanism of a potent PEPT1 and PEPT2 inhibitor.Communications chemistry · 2022Article
- Novel variants provide differential stabilisation of human equilibrative nucleoside transporter 1 states.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
- Rapid and Sensitive Quantification of Intracellular Glycyl-Sarcosine for Semi-High-Throughput Screening for Inhibitors of PEPT-1.Pharmaceutics · 2021Article
- Insights into the Role of the Discontinuous TM7 Helix of Human Ferroportin through the Prism of the Asp325 Residue.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
Proton-coupled oligopeptide transporters belong to the major facilitator superfamily (MFS) of membrane transporters. Recent crystal structures suggest the MFS fold facilitates transport through rearrangement of their two six-helix bundles around a central ligand binding site; how this is achieved, however, is poorly understood. Using modeling, molecular dynamics, crystallography, functional assays, and site-directed spin labeling combined with double electron-electron resonance (DEER) spectroscopy, we present a detailed study of the transport dynamics of two bacterial oligopeptide transporters, PepTSo and PepTSt. Our results identify several salt bridges that stabilize outward-facing conformations and we show that, for all the current structures of MFS transporters, the first two helices of each of the four inverted-topology repeat units form half of either the periplasmic or cytoplasmic gate and that these function cooperatively in a scissor-like motion to control access to the peptide binding site during transport.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.