Journal
FEBS LETTERS
Volume 505, Issue 3, Pages 353-356Publisher
WILEY
DOI: 10.1016/S0014-5793(01)02837-X
Keywords
ATP synthase; subunit c ring; phospholipid; atomic force microscopy; Hyobacter tartaricus
Ask authors/readers for more resources
The isolated rotor cylinder of the ATP synthase from Ilyobacter tartaricus was reconstituted into two-dimensional crystalline arrays. Atomic force microscopy imaging indicated a central cavity on one side of the rotor and a central plug protruding from the other side. Upon incubation with phospholipase C, the plug disappeared, but the appearance of the surrounding c subunit oligomer was not affected. This indicates that the plug consists of phospholipids. As the detergent-purified c cylinder is completely devoid of phospholipids, these are incorporated into the central hole from one side of the cylinder during the reconstitution procedure. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available