Molecular architecture of the rotary motor in ATP synthase - PubMed (original) (raw)
Molecular architecture of the rotary motor in ATP synthase
D Stock et al. Science. 1999.
Abstract
Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.
Comment in
- Molecular rotary motors.
Fillingame RH. Fillingame RH. Science. 1999 Nov 26;286(5445):1687-8. doi: 10.1126/science.286.5445.1687. Science. 1999. PMID: 10610565 No abstract available.
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