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TitleOutward open conformation of a Major Facilitator Superfamily multidrug/H+antiporter provides insights into switching mechanism.
Journal, issue, pagesNat Commun, Vol. 9, Page 4005-4005, Year 2018
Publish dateJun 20, 2018 (structure data deposition date)
AuthorsNagarathinam, K. / Nakada-Nakura, Y. / Parthier, C. / Terada, T. / Juge, N. / Jaenecke, F. / Liu, K. / Hotta, Y. / Miyaji, T. / Omote, H. ...Nagarathinam, K. / Nakada-Nakura, Y. / Parthier, C. / Terada, T. / Juge, N. / Jaenecke, F. / Liu, K. / Hotta, Y. / Miyaji, T. / Omote, H. / Iwata, S. / Nomura, N. / Stubbs, M.T. / Tanabe, M.
External linksNat Commun / PubMed:30275448
MethodsX-ray diffraction
Resolution3.4 Å
Structure data

PDB-6gv1:
Crystal structure of E.coli Multidrug/H+ antiporter MdfA in outward open conformation with bound Fab fragment
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

Chemicals

ChemComp-SO4:
SULFATE ION

Source
  • escherichia coli k-12 (bacteria)
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / Major Facilitator Superfamily / multidrug resistance / proton transport / MFS transporter / drug proton antiporter

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