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TitleA cation-pi interaction in a transmembrane helix of vacuolar ATPase retains the proton-transporting arginine in a hydrophobic environment.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 18977-18988, Year 2018
Publish dateAug 24, 2018 (structure data deposition date)
AuthorsHohlweg, W. / Wagner, G.E. / Hofbauer, H.F. / Sarkleti, F. / Setz, M. / Gubensak, N. / Lichtenegger, S. / Falsone, S.F. / Wolinski, H. / Kosol, S. ...Hohlweg, W. / Wagner, G.E. / Hofbauer, H.F. / Sarkleti, F. / Setz, M. / Gubensak, N. / Lichtenegger, S. / Falsone, S.F. / Wolinski, H. / Kosol, S. / Oostenbrink, C. / Kohlwein, S.D. / Zangger, K.
External linksJ. Biol. Chem. / PubMed:30209131
MethodsNMR (solution)
Structure data

PDB-6hh0:
Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles
Method: SOLUTION NMR

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsMEMBRANE PROTEIN / ATPasse / transmembrane helix / DPC micelle / NMR spectroscopy

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