Structural basis for polyspecificity in the POT family of proton-coupled oligopeptide transporters
Citation:
Lyons, 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 Reports, 15, 8, 2014, 886 - 893Download Item:
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Abstract:
An enigma in the field of peptide transport is the structural basis for
ligand promiscuity, as exemplified by PepT
1, 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.
Sponsor
Grant Number
Science Foundation Ireland (SFI)
12 /IA/ 1255
Science Foundation Ireland (SFI)
07/IN.1/B1836
Author's Homepage:
http://people.tcd.ie/mcaffreDescription:
PUBLISHED
Author: CAFFREY, MARTIN
Type of material:
Journal ArticleCollections:
Series/Report no:
EMBO Reports15
8
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Full text availableDOI:
http://dx.doi.org/10.15252/embr.201338403Licences: