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J. Biol. Chem., Vol. 278, Issue 23, 21162-21167, June 6, 2003

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The Membrane Domain of the Na⁺-motive V-ATPase from Enterococcus hirae Contains a Heptameric Rotor^*

Takeshi Murata  , Ignacio Arechaga  , Ian M. Fearnley , Yoshimi Kakinuma ¶, Ichiro Yamato || and John E. Walker  **

From the Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, United Kingdom, the ^¶Department of Applied Chemistry, Muroran Institute of Technology, 27-1 Mizumoto-cho, Muroran-shi, Hokkaido 050-8585, Japan, and the ^||Department of Biological Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda-shi, Chiba 278-8510, Japan

In F-ATPases, ATP hydrolysis is coupled to translocation of ions through membranes by rotation of a ring of c subunits in the membrane. The ring is attached to a central shaft that penetrates the catalytic domain, which has pseudo-3-fold symmetry. The ion translocation pathway lies between the external circumference of the ring and another hydrophobic protein. The H⁺ or Na⁺:ATP ratio depends upon the number of ring protomers, each of which has an essential carboxylate involved directly in ion translocation. This number and the ratio differ according to the source, and 10, 11, and 14 protomers have been found in various enzymes, with corresponding calculated H⁺ or Na⁺:ATP ratios of 3.3, 3.7, and 4.7. V-ATPases are related in structure and function to F-ATPases. Oligomers of subunit K from the Na⁺-motive V-ATPase of Enterococcus hirae also form membrane rings but, as reported here, with 7-fold symmetry. Each protomer has one essential carboxylate. Thus, hydrolysis of one ATP provides energy to extrude 2.3 sodium ions. Symmetry mismatch between the catalytic and membrane domains appears to be an intrinsic feature of both V- and F-ATPases.

Received for publication, February 14, 2003 , and in revised form, March 14, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors contributed equally to this work.

^** To whom correspondence should be addressed. Tel.: 44-1223-252701; Fax: 44-1223-252705; E-mail: walker{at}mrc-dunn.cam.ac.uk.

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