Features of V-ATPases that distinguish them from F-ATPases.
The general structure of F- and V-ATPases is quite similar and they may share a common mechanism of action that involves mechanochemical energy transduction. Both holoenzymes are composed of catalytic sectors, F1 and V1 respectively, and membrane sectors, F(o) and V(o) respectively. Although we assume that a similar mechanism underlies ATP-dependent proton pumping by F- and V-ATPases in eukaryotic cells, the latter cannot catalyze pmf-driven ATP synthesis. The loss of this ability is probably due to a proton slip that is a consequence of alterations in its membrane sector. The major events include gene duplication of the proteolipids and the presence of three distinct proteolipids in each complex.
Perzov
N
N
Department of Biochemistry, The George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978, Tel Aviv, Israel.
Padler-Karavani
V
V
Nelson
H
H
Nelson
N
N
D000255:Adenosine Triphosphate / Q000096:biosynthesis / Q000378:metabolism; D020134:Catalytic Domain; D002462:Cell Membrane / Q000737:chemistry; D007202:Indicators and Reagents / Q000494:pharmacology; D008954:Models, Biological; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011510:Proteolipids / Q000737:chemistry; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D011522:Protons; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D025262:Vacuolar Proton-Translocating ATPases
D007202:Indicators and Reagents; D011510:Proteolipids; D011522:Protons; D011993:Recombinant Fusion Proteins; D000255:Adenosine Triphosphate; D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases