Composition of the central stalk of the Na+-pumping V-ATPase from Caloramator fervidus.
The Na+-pumping V-ATPase complex of the thermophilic bacterium Caloramator fervidus was purified and dissociated under controlled conditions. The structure of purified V1-ATPase subcomplexes differing in subunit composition was analyzed by electron microscopy and single particle analysis of 50 000 projections. Difference mapping of subcomplex projections revealed the presence and position of two subunits in the central stalk. A density with an elongated shape similar to the gamma subunit of F-ATPases is partly located within V1 and corresponds, most likely, to subunit E. Subunit E is connected to the membrane-bound part V0 via subunit C, a spherical density that is connected to the center of V0. The presence of subunit C makes the central stalk substantially longer in comparison to the F-ATPases, in which the gamma subunit connects directly to F0.
Chaban
Yuriy
Y
Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands.
Ubbink-Kok
Trees
T
Keegstra
Wilko
W
Lolkema
Juke S
JS
Boekema
Egbert J
EJ
D001426:Bacterial Proteins / Q000737:chemistry; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D016937:Gram-Positive Endospore-Forming Rods / Q000201:enzymology*; D008854:Microscopy, Electron; D017434:Protein Structure, Tertiary; D012964:Sodium / Q000378:metabolism*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000302:isolation & purification*
D001426:Bacterial Proteins; D012964:Sodium; D025262:Vacuolar Proton-Translocating ATPases