Rotor architecture in the yeast and bovine F1-c-ring complexes of F-ATP synthase

• Published in: Journal of structural biology 2012-02, Vol.177 (2), p.490-497
• Main Authors: Giraud, Marie-France, Paumard, Patrick, Sanchez, Corinne, Brèthes, Daniel, Velours, Jean, Dautant, Alain
• Format: Article
• Language: English
• Subjects: Animals; Cattle; Cellular Biology; Crystal structure; Crystallography, X-Ray; F1FO-ATP synthase; Life Sciences; Models, Molecular; Molecular motor; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Proton-Translocating ATPases - chemistry; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae Proteins - chemistry; Structural Homology, Protein; Surface Properties
• ISSN: 1047-8477; 1095-8657
• DOI: 10.1016/j.jsb.2011.10.015

The F1FO-ATP synthase is a rotary molecular nanomotor. F1 is a chemical motor driven by ATP hydrolysis while FO is an electrical motor driven by the proton flow. The two stepping motors are mechanically coupled through a common rotary shaft. Up to now, the three available crystal structures of the F1c10 sub-complex of the yeast F1FO-ATP synthase were isomorphous and then named yF1c10(I). In this crystal form, significant interactions of the c10-ring with the F1-head of neighboring molecules affected the overall conformation of the F1-c-ring complex. The symmetry axis of the F1-head and the inertia axis of the c-ring were tilted near the interface between the F1-central stalk and the c-ring rotor, resulting in an unbalanced machine. We have solved a new crystal form of the F1c10 complex, named yF1c10(II), inhibited by adenylyl-imidodiphosphate (AMP-PNP) and dicyclohexylcarbodiimide (DCCD), at 6.5Å resolution in which the crystal packing has a weaker influence over the conformation of the F1-c-ring complex. yF1c10(II) provides a model of a more efficient generator. yF1c10(II) and bovine bF1c8 structures share a common rotor architecture with the inertia center of the F1-stator close to the rotor axis.