FEBS Letters | |
The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids | |
Matthey, Ulrich2  Dimroth, Peter2  Henzen, Fabienne2  Meier, Thomas2  Müller, Daniel J.1  | |
[1] Max-Planck-Institute of Molecular Cell Biology and Genetics, D-01307 Dresden, Germany;Institut für Mikrobiologie, Eidgenössische Technische Hochschule, ETH-Zentrum, CH-8092 Zürich, Switzerland | |
关键词: ATP synthase; Subunit c ring; Phospholipid; Atomic force microscopy; Ilyobacter tartaricus; AFM; atomic force microscopy; SDS; sodium dodecyl sulfate; | |
DOI : 10.1016/S0014-5793(01)02837-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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