ArticleThe EMBO journal2012
Alternating access mechanism in the POT family of oligopeptide transporters.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.
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Who cites it
121 citing papers in PubMed, 243 citations in OpenAlex.
- Dipeptide Transport Systems at the Interface of Peptide Metabolism and Drug Delivery in Cancer.International journal of molecular sciences · 2026Review
- Structural basis of glucosinolate recognition and transport by plant GTR1.Cell discovery · 2026Article
- Functional characterization of NRT1/PTR FAMILY transporters: looking for a needle in a haystack.The New phytologist · 2026Review
- Defined roles for the Staphylococcus aureus POT transporter DtpT in di/tripeptide uptake and glutathione utilisation inside human macrophages.PLoS pathogens · 2025Article
- Conformational Landscape of the Di- and Tripeptide Permease A Transport Cycle.Journal of chemical information and modeling · 2025Article
- Structure and transport mechanism of human riboflavin transporters.Nature communications · 2025Article
- Energetics of substrate transport in proton-dependent oligopeptide transporters.Communications chemistry · 2024Article
- Cryo-EM characterization of the anydromuropeptide permease AmpG central to bacterial fitness and β-lactam antibiotic resistance.Nature communications · 2024Article
- Structure and function ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural basis for antibiotic transport and inhibition in PepT2.Nature communications · 2024Article
- Article
- FOCUS on NOD2: Advancing IBD Drug Discovery with a User-Informed Machine Learning Framework.ACS medicinal chemistry letters · 2024Article
- Nitrate transporter protein NPF5.12 and major latex-like protein MLP6 are important defense factors against Verticillium longisporum.Journal of experimental botany · 2024Article
- Structural basis for antibiotic transport and inhibition in PepT2, the mammalian proton-coupled peptide transporter.Research square · 2024Article
- Orphan lysosomal solute carrier MFSD1 facilitates highly selective dipeptide transport.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Linking microbial genes to plasma and stool metabolites uncovers host-microbial interactions underlying ulcerative colitis disease course.Cell host & microbe · 2024Article
- Review
- Genome-wide identification and expression analysis of the NRT genes in Ginkgo biloba under nitrate treatment reveal the potential roles during calluses browning.BMC genomics · 2023Article
- 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
61 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Short chain peptides are actively transported across membranes as an efficient route for dietary protein absorption and for maintaining cellular homeostasis. In mammals, peptide transport occurs via PepT1 and PepT2, which belong to the proton-dependent oligopeptide transporter, or POT family. The recent crystal structure of a bacterial POT transporter confirmed that they belong to the major facilitator superfamily of secondary active transporters. Despite the functional characterization of POT family members in bacteria, fungi and mammals, a detailed model for peptide recognition and transport remains unavailable. In this study, we report the 3.3-Å resolution crystal structure and functional characterization of a POT family transporter from the bacterium Streptococcus thermophilus. Crystallized in an inward open conformation the structure identifies a hinge-like movement within the C-terminal half of the transporter that facilitates opening of an intracellular gate controlling access to a central peptide-binding site. Our associated functional data support a model for peptide transport that highlights the importance of salt bridge interactions in orchestrating alternating access within the POT family.
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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.