4TPH: Selectivity Mechanism Of A Bacterial Homologue Of The Human Drug Peptide Transporters Pept1 And Pept2

Peptide transporters of the PepT family have key roles in the transport of di- and tripeptides across membranes as well as in the absorption of orally administered drugs in the small intestine. We have determined structures of a PepT transporter from Shewanella oneidensis (PepT(So2)) in complex with three different peptides. The peptides bind in a large cavity lined by residues that are highly conserved in human PepT1 and PepT2. The bound peptides adopt extended conformations with their N termini clamped into a conserved polar pocket. A positively charged patch allows differential interactions with the C-terminal carboxylates of di- and tripeptides. Here we identify three pockets for peptide side chain interactions, and our binding studies define differential roles of these pockets for the recognition of different subtypes of peptide side chains.
PDB ID: 4TPHDownload
MMDB ID: 121405
PDB Deposition Date: 2014/6/7
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 3.16  Å
Source Organism:
Similar Structures:
Biological Unit for 4TPH: dimeric; determined by author and by software (PISA)
Molecular Components in 4TPH
Label Count Molecule
Proteins (2 molecules)
Proton:oligopeptide Symporter POT Family
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB