We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
On the structure of the stator of the mitochondrial ATP synthase.
- Authors
Dickson, Veronica Kane; Silvester, Jocelyn A; Fearnley, Ian M; Leslie, Andrew G W; Walker, John E
- 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.
- Publication
The EMBO journal, 2006, Vol 25, Issue 12, p2911
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1038/sj.emboj.7601177