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Structural insights into substrate recognition in proton‐dependent oligopeptide transporters
Author(s) -
Guettou Fatma,
Quistgaard Esben M,
Trésaugues Lionel,
Moberg Per,
Jegerschöld Caroline,
Zhu Lin,
Jong Agnes Jin Oi,
Nordlund Pär,
Löw Christian
Publication year - 2013
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2013.107
Subject(s) - major facilitator superfamily , oligopeptide , transporter , subfamily , biochemistry , shewanella oneidensis , tetrapeptide , chemistry , peptidomimetic , superfamily , biology , biophysics , peptide , bacteria , receptor , gene , genetics
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 (PepT So2 ), 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.