Search

The endogenous inhibitor of ATP synthase in mitochondria, called IF1, conserves cellular energy when the proton-motive force collapses by inhibiting ATP hydrolysis. Around neutrality, the 84-amino-acid bovine IF1 is thought to...

ATP hydrolysis inhibitor Intrinsically Disordered Protein Mitochondria regulation Amino Acids Animals Cattle Dimerization Hydrogen-Ion Concentration Hydrolysis Mitochondria Mitochondrial Proton-Translocating ATPases Protein Binding Protein Conformation alpha-Helical Proteins

The crystal structure of the F1-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially...

ATP hydrolysis Fusobacterium nucleatum catalytic F1-ATPase pathogen regulation structure Adenosine Diphosphate Bacterial Proteins Crystallography X-Ray Fusobacterium nucleatum Hydrolysis Models Molecular Molecular Conformation Protein Domains Proton-Translocating ATPases

DNA replicases utilize ring-shaped sliding clamps to ensure polymerase processivity. An ATP-dependent clamp loader topologically links the clamp around DNA in a multi-step mechanism. Clamp loaders are ring-shaped pentamers of...

DNA Replication clamp loaders ATP hydrolysis clamp proteins Life Sciences

Nucleoside triphosphates (NTPs) are used as chemical energy source in a variety of cell systems. Structural snapshots along the NTP hydrolysis reaction coordinate are typically obtained by adding stable, nonhydrolyzable...

ABC transporter ATP analogues ATP hydrolysis DnaB helicase ELDOR-detected NMR Solid-state NMR ATP-Binding Cassette Transporters Adenosine Triphosphatases Adenosine Triphosphate Adenylyl Imidodiphosphate Aluminum Compounds Bacillus subtilis Bacterial Proteins DnaB Helicases Electron Spin Resonance Spectroscopy ELECTRONS Fluorides Helicobacter pylori Hydrolysis Magnetic Resonance Spectroscopy Protein Conformation