On the structure of the stator of the mitochondrial ATP synthase.

TitleOn the structure of the stator of the mitochondrial ATP synthase.
Publication TypeJournal Article
Year of Publication2006
AuthorsDickson, VKane, Silvester, JA, Fearnley, IM, Leslie, AGW, Walker, JE
JournalEMBO J
Volume25
Issue12
Pagination2911-8
Date Published2006 Jun 21
ISSN0261-4189
KeywordsAnimals, Cattle, Crystallography, X-Ray, Mitochondrial Proton-Translocating ATPases, Models, Molecular
Abstract

The structure of most of the peripheral stalk, or stator, of the F-ATPase from bovine mitochondria, determined at 2.8 A resolution, contains residues 79-183, 3-123 and 5-70 of subunits b, d and F6, respectively. It consists of a continuous curved alpha-helix about 160 A long in the single b-subunit, augmented by the predominantly alpha-helical d- and F6-subunits. The structure occupies most of the peripheral stalk in a low-resolution structure of the F-ATPase. The long helix in subunit b extends from near to the top of the F1 domain to the surface of the membrane domain, and it probably continues unbroken across the membrane. Its uppermost region interacts with the oligomycin sensitivity conferral protein, bound to the N-terminal region of one alpha-subunit in the F1 domain. Various features suggest that the peripheral stalk is probably rigid rather than resembling a flexible rope. It remains unclear whether the transient storage of energy required by the rotary mechanism takes place in the central stalk or in the peripheral stalk or in both domains.

DOI10.1038/sj.emboj.7601177
Alternate JournalEMBO J.
Citation Key10.1038/sj.emboj.7601177
PubMed ID16791136
PubMed Central IDPMC1500866
Grant ListMC_U105184325 / / Medical Research Council / United Kingdom
MC_U105663148 / / Medical Research Council / United Kingdom