6O7T

Saccharomyces cerevisiae V-ATPase Vph1-VO

Summary for 6O7T

• Entry DOI: 10.2210/pdb6o7t/pdb
• Related: 6O7U 6O7V 6O7W 6O7X
• EMDB information: 0644 0645 0646 0647 0648
• Descriptor: V-type proton ATPase subunit a, vacuolar isoform, V0 assembly protein 1, V-type proton ATPase subunit c'', ... (8 entities in total)
• Functional Keywords: proton pump, membrane protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 15
• Total formula weight: 356135.56

Authors

Vasanthakumar, T.,Bueler, S.A.,Wu, D.,Beilsten-Edmands, V.,Robinson, C.V.,Rubinstein, J.L. (deposition date: 2019-03-08, release date: 2019-04-03, Last modification date: 2024-03-20)

Primary citation

Vasanthakumar, T.,Bueler, S.A.,Wu, D.,Beilsten-Edmands, V.,Robinson, C.V.,Rubinstein, J.L.
Structural comparison of the vacuolar and Golgi V-ATPases fromSaccharomyces cerevisiae.
Proc. Natl. Acad. Sci. U.S.A., 116:7272-7277, 2019

PubMed Abstract: Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal acidification. In mammals, V-ATPase subunit isoforms are differentially targeted to various intracellular compartments or tissues, but how these subunit isoforms influence enzyme activity is not clear. In the yeast , isoform diversity is limited to two different versions of the proton-translocating subunit a: Vph1p, which is targeted to the vacuole, and Stv1p, which is targeted to the Golgi apparatus and endosomes. We show that purified V-ATPase complexes containing Vph1p have higher ATPase activity than complexes containing Stv1p and that the relative difference in activity depends on the presence of lipids. We also show that V complexes containing Stv1p could be readily purified without attached V regions. We used this effect to determine structures of the membrane-embedded V region with Stv1p at 3.1-Å resolution, which we compare with a structure of the V region with Vph1p that we determine to 3.2-Å resolution. These maps reveal differences in the surface charge near the cytoplasmic proton half-channel. Both maps also show the presence of bound lipids, as well as regularly spaced densities that may correspond to ergosterol or bound detergent, around the c-ring.

PubMed: 30910982
DOI: 10.1073/pnas.1814818116

Experimental method

ELECTRON MICROSCOPY (3.2 Å)