title: The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids.
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.
authors.affiliation: Institut für Mikrobiologie, Eidgenössische Technische Hochschule, ETH-Zentrum, Zürich, Switzerland.
authors.forename: T
authors.initials: T
authors.lastname: Meier
authors.forename: U
authors.initials: U
authors.lastname: Matthey
authors.forename: F
authors.initials: F
authors.lastname: Henzen
authors.forename: P
authors.initials: P
authors.lastname: Dimroth
authors.forename: D J
authors.initials: DJ
authors.lastname: Müller
mesh_terms: D005673:Fusobacterium / Q000201:enzymology*; D018625:Microscopy, Atomic Force; D010743:Phospholipids / Q000737:chemistry*; D006180:Proton-Translocating ATPases / Q000737:chemistry*
chemical_list: D010743:Phospholipids; D006180:Proton-Translocating ATPases