Abstract
F- and V-type ATPases are central enzymes in energy metabolism that couple synthesis or hydrolysis of ATP to the translocation of H + or Na + across biological membranes. They consist of a soluble headpiece that contains the catalytic sites and an integral membrane-bound part that conducts the ion flow. Energy coupling is thought to occur through the physical rotation of a stalk that connects the two parts of the enzyme complex. This mechanism implies that a stator-like structure prevents the rotation of the headpiece relative to the membrane-bound part. Such a structure has not been observed to date. Here, we report the projected structure of the V-type Na + -ATPase of Clostridium fervidus as determined by electron microscopy. Besides the central stalk, a second stalk of 130 Å in length is observed that connects the headpiece and membrane-bound part in the periphery of the complex. This additional stalk is likely to be the stator.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 26, 2002, 10:35 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 2:26 p.m.) |
Indexed | 2 weeks, 3 days ago (Aug. 6, 2025, 9:24 a.m.) |
Issued | 27 years, 8 months ago (Dec. 23, 1997) |
Published | 27 years, 8 months ago (Dec. 23, 1997) |
Published Online | 27 years, 8 months ago (Dec. 23, 1997) |
Published Print | 27 years, 8 months ago (Dec. 23, 1997) |
@article{Boekema_1997, title={Visualization of a peripheral stalk in V-type ATPase: Evidence for the stator structure essential to rotational catalysis}, volume={94}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.94.26.14291}, DOI={10.1073/pnas.94.26.14291}, number={26}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Boekema, E. J. and Ubbink-Kok, T. and Lolkema, J. S. and Brisson, A. and Konings, W. N.}, year={1997}, month=dec, pages={14291–14293} }