doi: 10.1126/science.286.5445.1700.
Molecular architecture of the rotary motor in ATP synthase
Affiliations
- PMID:10576729
- DOI: 10.1126/science.286.5445.1700
Item in Clipboard
Molecular architecture of the rotary motor in ATP synthase
D Stock et al. Science..
Display options
Format
Display options
Format
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:10610565No abstract available.
Publication types
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases