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