Your browser doesn't support javascript.
loading
A cation-π interaction in a transmembrane helix of vacuolar ATPase retains the proton-transporting arginine in a hydrophobic environment.
Hohlweg, Walter; Wagner, Gabriel E; Hofbauer, Harald F; Sarkleti, Florian; Setz, Martina; Gubensäk, Nina; Lichtenegger, Sabine; Falsone, Salvatore Fabio; Wolinski, Heimo; Kosol, Simone; Oostenbrink, Chris; Kohlwein, Sepp D; Zangger, Klaus.
Afiliación
  • Hohlweg W; From the Institutes of Chemistry and.
  • Wagner GE; the Institute of Hygiene, Microbiology, and Environmental Medicine, Medical University of Graz, 8010 Graz, Austria.
  • Hofbauer HF; the Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, 8010 Graz, Austria.
  • Sarkleti F; the Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, 8010 Graz, Austria.
  • Setz M; the Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
  • Gubensäk N; From the Institutes of Chemistry and.
  • Lichtenegger S; the Institute of Hygiene, Microbiology, and Environmental Medicine, Medical University of Graz, 8010 Graz, Austria.
  • Falsone SF; Pharmaceutical Sciences, University of Graz, 8010 Graz, Austria.
  • Wolinski H; the Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, 8010 Graz, Austria.
  • Kosol S; the Department of Chemistry, University of Warwick, Gibbet Hill, Coventry CV4 7AL, United Kingdom.
  • Oostenbrink C; the Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
  • Kohlwein SD; the Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, 8010 Graz, Austria.
  • Zangger K; From the Institutes of Chemistry and klaus.zangger@uni-graz.at.
J Biol Chem ; 293(49): 18977-18988, 2018 12 07.
Article en En | MEDLINE | ID: mdl-30209131
Vacuolar ATPases are multisubunit protein complexes that are indispensable for acidification and pH homeostasis in a variety of physiological processes in all eukaryotic cells. An arginine residue (Arg735) in transmembrane helix 7 (TM7) of subunit a of the yeast ATPase is known to be essential for proton translocation. However, the specific mechanism of its involvement in proton transport remains to be determined. Arginine residues are usually assumed to "snorkel" toward the protein surface when exposed to a hydrophobic environment. Here, using solution NMR spectroscopy, molecular dynamics simulations, and in vivo yeast assays, we obtained evidence for the formation of a transient, membrane-embedded cation-π interaction in TM7 between Arg735 and two highly conserved nearby aromatic residues, Tyr733 and Trp737 We propose a mechanism by which the transient, membrane-embedded cation-π complex provides the necessary energy to keep the charged side chain of Arg735 within the hydrophobic membrane. Such cation-π interactions may define a general mechanism to retain charged amino acids in a hydrophobic membrane environment.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arginina / Protones / ATPasas de Translocación de Protón Vacuolares / Proteínas de Saccharomyces cerevisiae Idioma: En Revista: J Biol Chem Año: 2018 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arginina / Protones / ATPasas de Translocación de Protón Vacuolares / Proteínas de Saccharomyces cerevisiae Idioma: En Revista: J Biol Chem Año: 2018 Tipo del documento: Article Pais de publicación: Estados Unidos