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Originally published in Science Express on 31 March 2005
Science 29 April 2005:
Vol. 308. no. 5722, pp. 654 - 659
DOI: 10.1126/science.1110064
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Research Articles

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

Takeshi Murata,1 Ichiro Yamato,2 Yoshimi Kakinuma,3 Andrew G. W. Leslie,4* John E. Walker1*

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 F1Fo- or F-ATPases, respectively. Each NtpK subunit has four transmembrane {alpha} 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.

1 The Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.
2 Department of Biological Science and Technology, Tokyo University of Science, Chiba, 278-8510, Japan.
3 Faculty of Agriculture, Ehime University, Matsuyama 790-8566, Japan.
4 The Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.

* To whom correspondence should be addressed. E-mail: walker{at}mrc-dunn.cam.ac.uk (J.E.W.); andrew{at}mrc-lmb.cam.ac.uk (A.G.W.L.)

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