Structural insights into substrate recognition in proton-dependent oligopeptide transporters.

Guettou F, Quistgaard EM, Trésaugues L, Moberg P, Jegerschöld C, Zhu L, Jong AJ, Nordlund P, Löw C

EMBO Rep. 14 (9) 804-810 [2013-09-00; online 2013-07-23]

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.

Protein Science Facility (PSF)

QC bibliography QC xrefs

PubMed 23867627

DOI 10.1038/embor.2013.107

Crossref 10.1038/embor.2013.107

PDB 4LEP

embor2013107

pmc PMC3790050