title: Making the right moves.
abstract: The structure of the nucleotide-free F(1)-ATPase from a thermoalkaliphilic bacterium presented in this issue of Structure (Stocker et al., 2007) reveals the structural interactions that prevent the enzyme from operating naturally in the hydrolytic direction. The data provide new insights into the mechanism of the F(o)F(1)-ATP synthase.
authors: Mario A
authors: MA
authors: Bianchet
authors: L Mario
authors: LM
authors: Amzel
mesh_terms: D000255:Adenosine Triphosphate / Q000096:biosynthesis; D019943:Amino Acid Substitution; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D018698:Glutamic Acid / Q000378:metabolism; D006868:Hydrolysis; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D008954:Models, Biological; D011487:Protein Conformation; D012399:Rotation
chemical_list: D018698:Glutamic Acid; D000255:Adenosine Triphosphate; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases