The membrane domain of the Na+-motive V-ATPase from Enterococcus hirae contains a heptameric rotor.

TitleThe membrane domain of the Na+-motive V-ATPase from Enterococcus hirae contains a heptameric rotor.
Publication TypeJournal Article
Year of Publication2003
AuthorsMurata, T, Arechaga, I, Fearnley, IM, Kakinuma, Y, Yamato, I, Walker, JE
JournalJ Biol Chem
Volume278
Issue23
Pagination21162-7
Date Published2003 Jun 06
ISSN0021-9258
KeywordsAmino Acid Sequence, Cell Membrane, Enterococcus, Microscopy, Electron, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Tertiary, Sodium, Vacuolar Proton-Translocating ATPases
Abstract

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.

DOI10.1074/jbc.M301620200
Alternate JournalJ. Biol. Chem.
Citation Key10.1074/jbc.M301620200
PubMed ID12651848