4LEP

Structural insights into substrate recognition in proton dependent oligopeptide transporters

Summary for 4LEP

• Entry DOI: 10.2210/pdb4lep/pdb
• Descriptor: Proton:oligopeptide symporter POT family, N-[(1R)-1-phosphonoethyl]-L-alaninamide, ZINC ION (3 entities in total)
• Functional Keywords: mfs superfamily, peptide transporter, membrane protein, tranport protein
• Biological source: Shewanella oneidensis
• Total number of polymer chains: 2
• Total formula weight: 114906.00

Authors

Guettou, F.,Quistgaard, E.M.,Tresaugues, L.,Moberg, P.,Jegerschold, C.,Zhu, L.,Jong, A.J.,Nordlund, P.,Low, C. (deposition date: 2013-06-26, release date: 2013-07-10, Last modification date: 2024-02-28)

Primary citation

Guettou, F.,Quistgaard, E.M.,Tresaugues, L.,Moberg, P.,Jegerschold, C.,Zhu, L.,Jong, A.J.,Nordlund, P.,Low, C.
Structural insights into substrate recognition in proton-dependent oligopeptide transporters.
Embo Rep., 14:804-810, 2013

PubMed Abstract: 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.

PubMed: 23867627
DOI: 10.1038/embor.2013.107

Experimental method

X-RAY DIFFRACTION (3.2 Å)