|Title||Molecular architecture of the rotary motor in ATP synthase.|
|Publication Type||Journal Article|
|Year of Publication||1999|
|Authors||Stock, D, Leslie, AG, Walker, JE|
|Date Published||1999 Nov 26|
|Keywords||Adenosine Triphosphate, Catalysis, Crystallization, Crystallography, X-Ray, Hydrogen Bonding, Mitochondria, Models, Molecular, Molecular Motor Proteins, Protein Conformation, Protein Folding, Protein Structure, Secondary, Proton-Motive Force, Proton-Translocating ATPases, Protons, Saccharomyces cerevisiae|
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.