BIOCHEMISTRY: Filled with Lipids

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Science  10 Feb 2006:
Vol. 311, Issue 5762, pp. 743b
DOI: 10.1126/science.311.5762.743b

The F- and V-type proton-pumping ATPases exhibit a common mechanical design in which the transmembrane passage of protons turns a membrane-embedded rotor that drives the nucleotide-binding components of the cytoplasmic turret through a cycle of conformational changes. This motor can run in forward or reverse directions, hydrolyzing ATP as it pumps protons uphill or making ATP as protons flow downhill. The precise structure of the entire membrane assembly has not yet been determined, but recent findings have offered views of the homo-oligomeric ring, which contains from 10 to 14 identical c subunits, depending on species. Using a photogenerated carbene, Oberfeld et al. fill in one of the gaps by demonstrating that in the Escherichia coli F-ATPase, the c subunits can be crosslinked to phospholipids at the inner surface of the ring, which is large enough (about 15 to 20 Å in diameter) to accommodate about 10 lipid molecules in the outer leaflet and 2 or 3 in the inner leaflet. — GJC

Biochemistry 10.1021/bi052304+ (2006).

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