4lep

Structural insights into substrate recognition in proton dependent oligopeptide transportersStructural insights into substrate recognition in proton dependent oligopeptide transporters

Structural highlights 4lep is a 2 chain structure with sequence from Shewanella oneidensis MR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8EHE6_SHEON Publication Abstract from PubMed 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. Structural insights into substrate recognition in proton-dependent oligopeptide transporters.,Guettou F, Quistgaard EM, Tresaugues L, Moberg P, Jegerschold C, Zhu L, Jong AJ, Nordlund P, Low C EMBO Rep. 2013 Jul 19. doi: 10.1038/embor.2013.107. PMID:23867627 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Symporter 3D structures

spinqualitylabelsall models 4lep, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image