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Cited by 354

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Structure of the Rotor of the V-Type Na + -ATPase from Enterococcus hirae

Murata, Takeshi, Yamato, Ichiro, Kakinuma, Yoshimi, Leslie, Andrew G. W., Walker, John E.·2005·Science

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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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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CoChat. (2026). Citation check: Structure of the Rotor of the V-Type Na + -ATPase from Enterococcus hirae. https://app.cochat.ai/papers/10.1126/science.1110064
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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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