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Composition of the central stalk of the Na + ‐pumping V‐ATPase from Caloramator fervidus
Author(s) -
Chaban Yuriy,
UbbinkKok Trees,
Keegstra Wilko,
Lolkema Juke S,
Boekema Egbert J
Publication year - 2002
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kvf196
Subject(s) - stalk , protein subunit , atpase , gamma subunit , biophysics , pi , electron microscope , biology , crystallography , chemistry , biochemistry , enzyme , physics , optics , gene , horticulture
The Na + ‐pumping V‐ATPase complex of the thermophilic bacterium Caloramator fervidus was purified and dissociated under controlled conditions. The structure of purified V 1 ‐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 γ subunit of F‐ATPases is partly located within V 1 and corresponds, most likely, to subunit E. Subunit E is connected to the membrane‐bound part V 0 via subunit C, a spherical density that is connected to the center of V 0 . The presence of subunit C makes the central stalk substantially longer in comparison to the F‐ATPases, in which the γ subunit connects directly to F 0 .