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. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Meier, T., Matthey, U., Henzen, F., Dimroth, P., & Müller, D. J. (2001). The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids. FEBS Letters, 505(3), 353–356. https://doi.org/10.1016/S0014-5793(01)02837-X