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TitleAffinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector.
Journal, issue, pagesJ Biol Chem, Vol. 290, Issue 46, Page 27959-27971, Year 2015
Publish dateNov 13, 2015
AuthorsSergio Couoh-Cardel / Elena Milgrom / Stephan Wilkens /
PubMed AbstractThe membrane sector (Vo) of the proton pumping vacuolar ATPase (V-ATPase, V1Vo-ATPase) from Saccharomyces cerevisiae was purified to homogeneity, and its structure was characterized by EM of single ...The membrane sector (Vo) of the proton pumping vacuolar ATPase (V-ATPase, V1Vo-ATPase) from Saccharomyces cerevisiae was purified to homogeneity, and its structure was characterized by EM of single molecules and two-dimensional crystals. Projection images of negatively stained Vo two-dimensional crystals showed a ring-like structure with a large asymmetric mass at the periphery of the ring. A cryo-EM reconstruction of Vo from single-particle images showed subunits a and d in close contact on the cytoplasmic side of the proton channel. A comparison of three-dimensional reconstructions of free Vo and Vo as part of holo V1Vo revealed that the cytoplasmic N-terminal domain of subunit a (aNT) must undergo a large conformational change upon enzyme disassembly or (re)assembly from Vo, V1, and subunit C. Isothermal titration calorimetry using recombinant subunit d and aNT revealed that the two proteins bind each other with a Kd of ~5 μm. Treatment of the purified Vo sector with 1-palmitoyl-2-hydroxy-sn-glycero-3-[phospho-rac-(1-glycerol)] resulted in selective release of subunit d, allowing purification of a VoΔd complex. Passive proton translocation assays revealed that both Vo and VoΔd are impermeable to protons. We speculate that the structural change in subunit a upon release of V1 from Vo during reversible enzyme dissociation plays a role in blocking passive proton translocation across free Vo and that the interaction between aNT and d seen in free Vo functions to stabilize the Vo sector for efficient reassembly of V1Vo.
External linksJ Biol Chem / PubMed:26416888 / PubMed Central
MethodsEM (single particle)
Resolution18.0 Å
Structure data

EMDB-2975:
Cryo electron microscopy of yeast vacuolar ATPase proton channel sector
Method: EM (single particle) / Resolution: 18.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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