Rachael M Barry, Anne-Florence Bitbol ... Zemer Gitai
The accumulation of its product, cytidine triphosphate, encourages the enzyme CTP synthetase (CtpS) to form large-scale polymers and inhibits the enzyme's activity.
MgADP binding to the high-affinity 'consensus' ATPase active site of SUR1 and remodeling of the L0-loop (lasso region) overrides tonic ATP inhibition of KATP channels.
Structural analysis of the ATP synthase – in combination with evolutionary covariance analysis – reveals the fold of the a subunit and shows that the enzyme can adopt several different conformations, which support the Brownian ratchet model for generating rotation.
A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy.
Biochemical analysis on hetero-mutated c10 subunits ring and molecular dynamics simulations demonstrate the cooperation among c-subunits of FoF1-ATP synthase in rotation-coupled proton translocation.
A structural and biochemical approach shows that CTP binding and hydrolysis regulate nucleation, spreading, and recycling of a chromosome segregation protein ParB.
Michael H Hayes, Elizabeth H Peuchen ... Daniel L Weeks
The equilibrium between solubility and aggregation of proteins in the nucleus is controlled by co-aggregates like RNA and the action of ATP as both an energy source and a destabilizing chemical agent.
Meghna Sobti, Robert Ishmukhametov ... Alastair G Stewart
Cryo-EM studies reveal that incubation with ATP produces conformational intermediates of E. coli ATP synthase, in which the ε subunit is no longer in its autoinhibitory conformation.
Jesse M Hansen, Avital Horowitz ... Justin M Kollman
The yeast enzyme CTP synthase assembles inactive filaments that are driven to polymerization through the drop in cytoplasmic pH accompanying starvation.
Gregory M Martin, Balamurugan Kandasamy ... Show-Ling Shyng
A structure of a pancreatic ATP-sensitive potassium channel complex at 3.63Å resolution obtained by cryo-electron microscopy reveals how a commonly used anti-diabetic drug interacts with and inhibits the channel to stimulate insulin secretion.