Mechanism for allosteric inhibition of an ATP-sensitive ribozyme

摘要: We report the structural basis for modulation of an ATP-sensitive ribozyme that was engineered by modular rational design. This allosteric is composed two independently functioning domains, one a receptor ATP and other self-cleaving ribozyme. When fused in appropriate fashion, conjoined aptamer-ribozyme construct functions as inhibited presence ATP. The aptamer domain remains conformationally heterogeneous absence ATP, but folds into distinct structure upon ligand binding. ATP-induced conformational change causes reduction catalytic activity adjacent due to steric interference between tertiary structures. mechanism functional nucleic acids several possible mechanisms which function ribozymes could be specifically controlled small effector molecules.