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4D2C

Structure of a di peptide bound POT family peptide transporter

Summary for 4D2C
Entry DOI10.2210/pdb4d2c/pdb
Related4D2B 4D2D
DescriptorDi-or tripeptide:H+ symporter, (2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE, (2R)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE, ... (7 entities in total)
Functional Keywordstransport protein, major facilitator superfamily, proton oligopeptide transporter (pot) family, peptide transporter, peptide complex
Biological sourceStreptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Total number of polymer chains1
Total formula weight55957.14
Authors
Lyons, J.A.,Parker, J.L.,Solcan, N.,Brinth, A.,Li, D.,Shah, S.T.A.,Caffrey, M.,Newstead, S. (deposition date: 2014-05-09, release date: 2014-06-25, Last modification date: 2023-12-20)
Primary citationLyons, J.A.,Parker, J.L.,Solcan, N.,Brinth, A.,Li, D.,Shah, S.T.,Caffrey, M.,Newstead, S.
Structural Basis for Polyspecificity in the Pot Family of Proton-Coupled Oligopeptide Transporters.
Embo Rep., 15:886-, 2014
Cited by
PubMed Abstract: 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.
PubMed: 24916388
DOI: 10.15252/EMBR.201338403
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.47 Å)
Structure validation

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