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Structure paper

TitleSelectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 21, Page 728-, Year 2014
Publish dateJun 7, 2014 (structure data deposition date)
AuthorsGuettou, F. / Quistgaard, E.M. / Raba, M. / Moberg, P. / Low, C. / Nordlund, P.
External linksNat. Struct. Mol. Biol. / PubMed:25064511
MethodsX-ray diffraction
Resolution3.155 - 3.91 Å
Structure data

PDB-4tpg:
Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PepT1 and PepT2
Method: X-RAY DIFFRACTION / Resolution: 3.91 Å

PDB-4tph:
Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PepT1 and PepT2
Method: X-RAY DIFFRACTION / Resolution: 3.155 Å

PDB-4tpj:
Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PepT1 and PepT2
Method: X-RAY DIFFRACTION / Resolution: 3.201 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-ALA:
ALANINE

ChemComp-DBY:
3,5 DIBROMOTYROSINE

Source
  • shewanella oneidensis mr-1 (bacteria)
  • synthetic construct (others)
  • shewanella oneidensis (bacteria)
KeywordsMEMBRANE PROTEIN / complex / secondary active transporter

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