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PDBsum entry 4d2c
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Transport protein
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PDB id
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4d2c
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PDB id:
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| Name: |
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Transport protein
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Title:
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Structure of a di peptide bound pot family peptide transporter
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Structure:
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Di-or tripeptide:h+ symporter. Chain: a. Engineered: yes
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Source:
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Streptococcus thermophilus (strain atcc baa-250 / lmg 18311). Organism_taxid: 264199. Strain: atcc baa-250 / lmg 18311. Atcc: baa-250. Gene: dtpt, stu0970. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: c43.
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Resolution:
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2.47Å
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R-factor:
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0.225
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R-free:
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0.266
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Authors:
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J.A.Lyons,J.L.Parker,N.Solcan,A.Brinth,D.Li,S.T.A.Shah,M.Caffrey, S.Newstead
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Key ref:
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J.A.Lyons
et al.
(2014).
Structural basis for polyspecificity in the POT family of proton-coupled oligopeptide transporters.
Embo Rep,
15,
886-893.
PubMed id:
DOI:
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Date:
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09-May-14
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Release date:
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25-Jun-14
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PROCHECK
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Headers
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References
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Q5M4H8
(Q5M4H8_STRT2) -
Di-or tripeptide:H+ symporter from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
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Seq:
Struc:
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483 a.a.
429 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Embo Rep
15:886-893
(2014)
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PubMed id:
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Structural basis for polyspecificity in the POT family of proton-coupled oligopeptide transporters.
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J.A.Lyons,
J.L.Parker,
N.Solcan,
A.Brinth,
D.Li,
S.T.Shah,
M.Caffrey,
S.Newstead.
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ABSTRACT
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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.
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Links
