The structure of the membrane extrinsic region of bovine ATP synthase.

TitleThe structure of the membrane extrinsic region of bovine ATP synthase.
Publication TypeJournal Article
Year of Publication2009
AuthorsRees, DM, Leslie, AGW, Walker, JE
JournalProc Natl Acad Sci U S A
Volume106
Issue51
Pagination21597-601
Date Published2009 Dec 22
ISSN1091-6490
KeywordsAnimals, Cattle, Mitochondrial Proton-Translocating ATPases, Models, Molecular, Oligomycins, Protein Conformation
Abstract

The structure of the complex between bovine mitochondrial F(1)-ATPase and a stator subcomplex has been determined at a resolution of 3.2 A. The resolved region of the stator contains residues 122-207 of subunit b; residues 5-25 and 35-57 of F(6); 3 segments of subunit d from residues 30-40, 65-74, and 85-91; and residues 1-146 and 169-189 of the oligomycin sensitivity conferral protein (OSCP). The stator subcomplex represents its membrane distal part, and its structure has been augmented with an earlier structure of a subcomplex containing residues 79-183, 3-123, and 5-70 of subunits b, d, and F(6), respectively, which extends to the surface of the inner membrane of the mitochondrion. The N-terminal domain of the OSCP links the stator with F(1)-ATPase via alpha-helical interactions with the N-terminal region of subunit alpha(E). Its C-terminal domain makes extensive helix-helix interactions with the C-terminal alpha-helix of subunit b from residues 190-207. Subunit b extends as a continuous 160-A long alpha-helix from residue 188 back to residue 79 near to the surface of the inner mitochondrial membrane. This helix appears to be stiffened by other alpha-helices in subunits d and F(6), but the structure can bend inward toward the F(1) domain around residue 146 of subunit b. The linker region between the 2 domains of the OSCP also appears to be flexible, enabling the stator to adjust its shape as it passes over the changing profile of the F(1) domain during a catalytic cycle. The structure of the membrane extrinsic part of bovine ATP synthase is now complete.

DOI10.1073/pnas.0910365106
Alternate JournalProc. Natl. Acad. Sci. U.S.A.
Citation Key10.1073/pnas.0910365106
PubMed ID19995987
PubMed Central IDPMC2789756
Grant ListMC_U105184325 / / Medical Research Council / United Kingdom
MC_U105663150 / / Medical Research Council / United Kingdom
/ / Medical Research Council / United Kingdom