Molecular architecture of the rotary motor in ATP synthase |
| |
Authors: | Stock D Leslie A G Walker J E |
| |
Affiliation: | Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|