Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT.

ABSTRACT: Proton-dependent oligopeptide transporters (POTs) are major facilitator superfamily (MFS) proteins that mediate the uptake of peptides and peptide-like molecules, using the inwardly directed H(+) gradient across the membrane. The human POT family transporter peptide transporter 1 is present in the brush border membrane of the small intestine and is involved in the uptake of nutrient peptides and drug molecules such as β-lactam antibiotics. Although previous studies have provided insight into the overall structure of the POT family transporters, the question of how transport is coupled to both peptide and H(+) binding remains unanswered. Here we report the high-resolution crystal structures of a bacterial POT family transporter, including its complex with a dipeptide analog, alafosfalin. Th

SUBMITTER: Doki S 

PROVIDER: S-EPMC3710879 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature