Mutations within the ATPase domain of RIG-I in patients with Singleton-Merten Syndrome prevent ATP-hydrolysis dependent dissociation of RIG-I from double-stranded RNA and lead to unintentional constitutive signaling through increased binding of endogenous RNA.
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.
The accumulation of its product, cytidine triphosphate, encourages the enzyme CTP synthetase (CtpS) to form large-scale polymers and inhibits the enzyme's activity.
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.
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.