The peripheral stalk of the mitochondrial ATP synthase.

TitleThe peripheral stalk of the mitochondrial ATP synthase.
Publication TypeJournal Article
Year of Publication2006
AuthorsWalker, JE, Dickson, VKane
JournalBiochim Biophys Acta
Volume1757
Issue5-6
Pagination286-96
Date Published2006 May-Jun
ISSN0006-3002
KeywordsAnimals, Bacteria, Catalytic Domain, Cattle, Chloroplasts, Mitochondrial Membranes, Mitochondrial Proton-Translocating ATPases, Models, Molecular, Protein Subunits, Submitochondrial Particles
Abstract

The peripheral stalk of F-ATPases is an essential component of these enzymes. It extends from the membrane distal point of the F1 catalytic domain along the surface of the F1 domain with subunit a in the membrane domain. Then, it reaches down some 45 A to the membrane surface, and traverses the membrane, where it is associated with the a-subunit. Its role is to act as a stator to hold the catalytic alpha3beta3 subcomplex and the a-subunit static relative to the rotary element of the enzyme, which consists of the c-ring in the membrane and the attached central stalk. The central stalk extends up about 45 A from the membrane surface and then penetrates into the alpha3beta3 subcomplex along its central axis. The mitochondrial peripheral stalk is an assembly of single copies of the oligomycin sensitivity conferral protein (the OSCP) and subunits b, d and F6. In the F-ATPase in Escherichia coli, its composition is simpler, and it consists of a single copy of the delta-subunit with two copies of subunit b. In some bacteria and in chloroplasts, the two copies of subunit b are replaced by single copies of the related proteins b and b' (known as subunits I and II in chloroplasts). As summarized in this review, considerable progress has been made towards establishing the structure and biophysical properties of the peripheral stalk in both the mitochondrial and bacterial enzymes. However, key issues are unresolved, and so our understanding of the role of the peripheral stalk and the mechanism of synthesis of ATP are incomplete.

DOI10.1016/j.bbabio.2006.01.001
Alternate JournalBiochim. Biophys. Acta
Citation Key10.1016/j.bbabio.2006.01.001
PubMed ID16697972
Grant ListMC_U105663150 / / Medical Research Council / United Kingdom