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The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids
Author(s) -
Meier Thomas,
Matthey Ulrich,
Henzen Fabienne,
Dimroth Peter,
Müller Daniel J.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02837-x
Subject(s) - atp synthase , cylinder , spark plug , rotor (electric) , chemistry , protein subunit , biophysics , enzyme , biochemistry , biology , geometry , physics , thermodynamics , mathematics , quantum mechanics , gene
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.