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Structure of the Rotor of the V-Type Na + -ATPase from Enterococcus hirae
Abstract
The membrane rotor ring from the vacuolar-type (V-type) sodium ion–pumping adenosine triphosphatase (Na + -ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in F 1 F o - or F-ATPases, respectively. Each NtpK subunit has four transmembrane α helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V- and F-ATPases.
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Cites
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Lee, A. G. (2003) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(03)00056-7 · Cited by 886
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Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
Watt, I. N., Montgomery, M. G., Runswick, M. J., Leslie, A. G. W., & Walker, J. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011099107 · Cited by 513
Self-citationEmerging Diversity in Lipid–Protein Interactions
Corradi, V., Sejdiu, B. I., Mesa-Galloso, H., Abdizadeh, H., Noskov, S. Y., Marrink, S. J., & Tieleman, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00451 · Cited by 459
Metadata
- Authors
- Murata, T., Yamato, I., Kakinuma, Y., Leslie, A. G. W., & Walker, J. E.
- Venue
- Science
- Published
- 2005-04-29
- Volume
- 308
- Issue
- 5722
- Pages
- 654-659
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2087094813
- Cited by
- 354
- References
- 1
- FWCI
- 11.87
- Type
- journal article
- Language
- en
- Open access
- closed
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- Murata, T., Yamato, I., Kakinuma, Y., Leslie, A. G. W., & Walker, J. E. (2005). Structure of the Rotor of the V-Type Na + -ATPase from Enterococcus hirae. Science. https://doi.org/10.1126/science.1110064
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