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Published Online March 31, 2005
Science DOI: 10.1126/science.1110064

Research Articles

Submitted on January 21, 2005
Accepted on March 8, 2005

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. Walker 1*

1 The MRC 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 MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.

* To whom correspondence should be addressed.
John E. Walker , E-mail: walker{at}mrc-dunn.cam.ac.uk

The membrane rotor ring from the Na+-pumping vacuolar type-ATPase from Enterococcus hirae consists of 10 NtpK subunits, homologs of the 16 kD and 8 kD proteolipids found in other vacuolar-ATPases and in F-ATPases, respectively. Each NtpK subunit has four transmembrane {alpha} helices, with a sodium ion bound between helices 2 and 4 at a site that includes the essential residue, Glu139. This site is buried deeply in the membrane. It is probably connected to the membrane surface via 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 vacuolar- and F-ATPases.


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