Molecular architecture of the rotary motor in ATP synthase.

TitleMolecular architecture of the rotary motor in ATP synthase.
Publication TypeJournal Article
Year of Publication1999
AuthorsStock, D, Leslie, AG, Walker, JE
JournalScience
Volume286
Issue5445
Pagination1700-5
Date Published1999 Nov 26
ISSN0036-8075
KeywordsAdenosine 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
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.

DOI10.1126/science.286.5445.1700
Alternate JournalScience
Citation Key10.1126/science.286.5445.1700
PubMed ID10576729