4d2c

Structure of a di peptide bound POT family peptide transporter

spinqualitylabelsall models 4d2c, resolution 2.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d2c is a 1 chain structure with sequence from Streptococcus thermophilus LMG 18311. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.47Å Ligands: 78M, 78N, ALA, PHE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5M4H8_STRT2 Publication Abstract from PubMed An enigma in the field of peptide transport is the structural basis for ligand promiscuity, as exemplified by PepT1, the mammalian plasma membrane peptide transporter. Here, we present crystal structures of di- and tripeptide-bound complexes of a bacterial homologue of PepT1, which reveal at least two mechanisms for peptide recognition that operate within a single, centrally located binding site. The dipeptide was orientated laterally in the binding site, whereas the tripeptide revealed an alternative vertical binding mode. The co-crystal structures combined with functional studies reveal that biochemically distinct peptide-binding sites likely operate within the POT/PTR family of proton-coupled symporters and suggest that transport promiscuity has arisen in part through the ability of the binding site to accommodate peptides in multiple orientations for transport. Structural basis for polyspecificity in the POT family of proton-coupled oligopeptide transporters.,Lyons JA, Parker JL, Solcan N, Brinth A, Li D, Shah ST, Caffrey M, Newstead S EMBO Rep. 2014 Jun 10. pii: e201338403. PMID:24916388 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Symporter Symporter 3D structures

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