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FEBS Lett. 2001 Sep 21;505(3):353-6.

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

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Institut für Mikrobiologie, Eidgenössische Technische Hochschule, ETH-Zentrum, Zürich, Switzerland.


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.

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