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Esben Meldgaard Høgh Quistgaard

Structural insights into substrate recognition in proton-dependent oligopeptide transporters

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DOI

  • Fatma Guettou, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, SE-17177, Stockholm, Sweden.
  • ,
  • Esben M Quistgaard
  • Lionel Trésaugues
  • ,
  • Per Moberg
  • ,
  • Caroline Jegerschöld
  • ,
  • Lin Zhu
  • ,
  • Agnes Jin Oi Jong
  • ,
  • Pär Nordlund
  • ,
  • Christian Löw

Short-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)--a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to target cells. Here, we present a structure of an oligomeric POT transporter from Shewanella oneidensis (PepTSo2), which was crystallized in the inward open conformation in complex with the peptidomimetic alafosfalin. All ligand-binding residues are highly conserved and the structural insights presented here are therefore likely to also apply to human POTs.

Original languageEnglish
JournalE M B O Reports
Volume14
Issue9
Pages (from-to)804-10
Number of pages7
ISSN1469-221X
DOIs
Publication statusPublished - Sep 2013
Externally publishedYes

    Research areas

  • Alanine, Amino Acid Sequence, Bacterial Proteins, Molecular Docking Simulation, Molecular Sequence Data, Protein Binding, Shewanella, Symporters, Journal Article

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