Structural basis for oligomerization of the prokaryotic peptide transporter PepT_So2.

ABSTRACT: Proton-dependent oligopeptide transporters (POTs) belong to the major facilitator superfamily (MFS) and transport dipeptides and tripeptides from the extracellular environment into the target cell. The human POTs PepT1 and PepT2 are also involved in the absorption of various orally ingested drugs. Previously reported structures revealed that the bacterial POTs possess 14 helices, of which H1-H6 and H7-H12 constitute the typical MFS fold and the residual two helices are involved in the cytoplasmic linker. PepT_So2 from Shewanella oneidensis is a unique POT which reportedly assembles as a 200 kDa tetramer. Although the previously reported structures suggested the importance of H12 for tetramer formation, the structural basis for the PepT_So2-specific oligomerization remai

SUBMITTER: Nagamura R 

PROVIDER: S-EPMC6497099 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature