The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids

54Citations
Citations of this article
37Readers
Mendeley users who have this article in their library.

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free