ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
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Who cites it
104 citing papers in PubMed, 199 citations in OpenAlex.
- Article
- Glycolipids slow interfacial proton migration while preserving surface proton retention.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural basis of glucosinolate recognition and polyspecific transport by the glucosinolate transporter GTR1.The Journal of biological chemistry · 2026Article
- Dipeptide Transport Systems at the Interface of Peptide Metabolism and Drug Delivery in Cancer.International journal of molecular sciences · 2026Review
- Energetics of substrate transport in proton-dependent oligopeptide transporters.Communications chemistry · 2024Article
- Article
- Linking microbial genes to plasma and stool metabolites uncovers host-microbial interactions underlying ulcerative colitis disease course.Cell host & microbe · 2024Article
- The impact of solute carrier proteins on disrupting substance regulation in metabolic disorders: insights and clinical applications.Frontiers in pharmacology · 2024Review
- Molecular Insights to the Structure-Interaction Relationships of Human Proton-Coupled Oligopeptide Transporters (PepTs).Pharmaceutics · 2023Review
- Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410.Nature communications · 2023Article
- Functional Characterization of the Putative POT fromBiology · 2023Article
- Ins and Outs of Rocker Switch Mechanism in Major Facilitator Superfamily of Transporters.Membranes · 2023Review
- Substrate-binding guides individual melibiose permeases MelB to structurally soften and to destabilize cytoplasmic middle-loop C3.Structure (London, England : 1993) · 2023Article
- Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport.Structure (London, England : 1993) · 2022Article
- Proton coupling and the multiscale kinetic mechanism of a peptide transporter.Biophysical journal · 2022Article
- Transport efficiency of AtGTR1 dependents on the hydrophobicity of transported glucosinolates.Scientific reports · 2022Article
- Peptide transporter structure reveals binding and action mechanism of a potent PEPT1 and PEPT2 inhibitor.Communications chemistry · 2022Article
- Concept of Fluorescent Transport Activity Biosensor for the Characterization of the Arabidopsis NPF1.3 Activity of Nitrate.Sensors (Basel, Switzerland) · 2022Article
- Structural Insights into the Substrate Transport Mechanisms in GTR Transporters through Ensemble Docking.International journal of molecular sciences · 2022Article
- Cryo-EM Structure of an Atypical Proton-Coupled Peptide Transporter: Di- and Tripeptide Permease C.Frontiers in molecular biosciences · 2022Article
44 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors at 6 institutions in 2 countries.
Funding
Abstract
Proton-dependent oligopeptide transporters (POTs) are major facilitator superfamily (MFS) proteins that mediate the uptake of peptides and peptide-like molecules, using the inwardly directed H(+) gradient across the membrane. The human POT family transporter peptide transporter 1 is present in the brush border membrane of the small intestine and is involved in the uptake of nutrient peptides and drug molecules such as β-lactam antibiotics. Although previous studies have provided insight into the overall structure of the POT family transporters, the question of how transport is coupled to both peptide and H(+) binding remains unanswered. Here we report the high-resolution crystal structures of a bacterial POT family transporter, including its complex with a dipeptide analog, alafosfalin. These structures revealed the key mechanistic and functional roles for a conserved glutamate residue (Glu310) in the peptide binding site. Integrated structural, biochemical, and computational analyses suggested a mechanism for H(+)-coupled peptide symport in which protonated Glu310 first binds the carboxyl group of the peptide substrate. The deprotonation of Glu310 in the inward open state triggers the release of the bound peptide toward the intracellular space and salt bridge formation between Glu310 and Arg43 to induce the state transition to the occluded conformation.
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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.