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PepT1 and PepT2 are major facilitator superfamily (MFS) transporters that utilize a proton gradient to drive the uptake of di- and tri-peptides in the small intestine and kidney, respectively. They are the major routes by which we absorb dietary nitrogen and many orally administered drugs. Here, we present the crystal structure of PepT So, a functionally similar prokaryotic homologue of the mammalian peptide transporters from Shewanella oneidensis. This structure, refined using data up to 3.6 Å resolution, reveals a ligand-bound occluded state for the MFS and provides new insights into a general transport mechanism. We have located the peptide-binding site in a central hydrophilic cavity, which occludes a bound ligand from both sides of the membrane. Residues thought to be involved in proton coupling have also been identified near the extracellular gate of the cavity. Based on these findings and associated kinetic data, we propose that PepT So represents a sound model system for understanding mammalian peptide transport as catalysed by PepT1 and PepT2. © 2011 European Molecular Biology Organization | All Rights Reserved.

Original publication

DOI

10.1038/emboj.2010.309

Type

Journal article

Journal

EMBO Journal

Publication Date

19/01/2011

Volume

30

Pages

417 - 426