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Science 26 November 1999:
Vol. 286. no. 5445, pp. 1700 - 1705
DOI: 10.1126/science.286.5445.1700
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Research Articles

Molecular Architecture of the Rotary Motor in ATP Synthase

Daniela Stock, 1 Andrew G. W. Leslie, 2 John E. Walker 1*

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.

1 Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.
2 Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
*   To whom correspondence should be addressed. E-mail: walker{at}mrc-dunn.cam.ac.uk

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   Abstract »    Full Text »    PDF »
Subunit rotation of ATP synthase embedded in membranes: a or beta subunit rotation relative to the c subunit ring.
K. Nishio, A. Iwamoto-Kihara, A. Yamamoto, Y. Wada, and M. Futai (2002)
PNAS 99, 13448-13452
   Abstract »    Full Text »    PDF »
Characterization of the First Cytoplasmic Loop of Subunit a of the Escherichia coli ATP Synthase by Surface Labeling, Cross-linking, and Mutagenesis.
J. C. Long, J. DeLeon-Rangel, and S. B. Vik (2002)
J. Biol. Chem. 277, 27288-27293
   Abstract »    Full Text »    PDF »
Mefloquine and New Related Compounds Target the F0 Complex of the F0F1 H+-ATPase of Streptococcus pneumoniae.
A. J. Martin-Galiano, B. Gorgojo, C. M. Kunin, and A. G. de la Campa (2002)
Antimicrob. Agents Chemother. 46, 1680-1687
   Abstract »    Full Text »    PDF »
Genetic Fusions of Globular Proteins to the epsilon Subunit of the Escherichia coli ATP Synthase. IMPLICATIONS FOR IN VIVO ROTATIONAL CATALYSIS AND epsilon SUBUNIT FUNCTION.
D. J. Cipriano, Y. Bi, and S. D. Dunn (2002)
J. Biol. Chem. 277, 16782-16790
   Abstract »    Full Text »    PDF »
Three-dimensional Map of a Plant V-ATPase Based on Electron Microscopy.
I. Domgall, D. Venzke, U. Luttge, R. Ratajczak, and B. Bottcher (2002)
J. Biol. Chem. 277, 13115-13121
   Abstract »    Full Text »    PDF »
F0 of ATP Synthase Is a Rotary Proton Channel. OBLIGATORY COUPLING OF PROTON TRANSLOCATION WITH ROTATION OF c-SUBUNIT RING.
T. Suzuki, H. Ueno, N. Mitome, J. Suzuki, and M. Yoshida (2002)
J. Biol. Chem. 277, 13281-13285
   Abstract »    Full Text »    PDF »
In the Absence of the First Membrane-spanning Segment of Subunit 4(b), the Yeast ATP Synthase Is Functional but Does Not Dimerize or Oligomerize.
V. Soubannier, J. Vaillier, P. Paumard, B. Coulary, J. Schaeffer, and J. Velours (2002)
J. Biol. Chem. 277, 10739-10745
   Abstract »    Full Text »    PDF »
Speed versus Efficiency in Microbial Growth and the Role of Parallel Pathways.
R. B. Helling (2002)
J. Bacteriol. 184, 1041-1045
   Abstract »    Full Text »    PDF »
Factor B and the Mitochondrial ATP Synthase Complex.
G. I. Belogrudov and Y. Hatefi (2002)
J. Biol. Chem. 277, 6097-6103
   Abstract »    Full Text »    PDF »
Membrane Topography of the Coupling Ion Binding Site in Na+-translocating F1F0 ATP Synthase.
C. von Ballmoos, Y. Appoldt, J. Brunner, T. Granier, A. Vasella, and P. Dimroth (2002)
J. Biol. Chem. 277, 3504-3510
   Abstract »    Full Text »    PDF »
The Conformation of the epsilon - and gamma -Subunits within the Escherichia coli F1 ATPase.
A. C. Hausrath, R. A. Capaldi, and B. W. Matthews (2001)
J. Biol. Chem. 276, 47227-47232
   Abstract »    Full Text »    PDF »
Three-dimensional Structure of the Vacuolar ATPase Proton Channel by Electron Microscopy.
S. Wilkens and M. Forgac (2001)
J. Biol. Chem. 276, 44064-44068
   Abstract »    Full Text »    PDF »
Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation.
S. Kawasaki-Nishi, T. Nishi, and M. Forgac (2001)
PNAS
   Abstract »    Full Text »    PDF »
Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the FO sector of Escherichia coli ATP synthase.
M. L. Hutcheon, T. M. Duncan, H. Ngai, and R. L. Cross (2001)
PNAS
   Abstract »    Full Text »    PDF »
Large conformational changes of the varepsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme.
S. P. Tsunoda, A. J. W. Rodgers, R. Aggeler, M. C. J. Wilce, M. Yoshida, and R. A. Capaldi (2001)
PNAS
   Abstract »    Full Text »    PDF »
The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.
W. Jiang, J. Hermolin, and R. H. Fillingame (2001)
PNAS 98, 4966-4971
   Abstract »    Full Text »    PDF »


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