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lüll Folding and catalysis by the hairpin ribozyme Lilley DMFEBS Lett 1999[Jun]; 452 (1-2): 26-30The hairpin ribozyme undergoes a site-specific transesterification cleavage of the phosphodiester backbone. The natural form of the ribozyme is a four-way helical junction, where two arms contain unpaired loops. This folds by pairwise coaxial stacking of helical arms, and a rotation into an antiparallel conformation in which there is close association between the loops. This probably generates the local conformation required to facilitate the trajectory into an in-line SN2 transition state. Folding is induced by the cooperative binding of at least two divalent metal ions, which are probably distributed between the junction and the loop-loop interface. The junction forms the structural scaffold on which the geometry of the ribozyme is built, and structural perturbation of the junction leads to impaired catalytic activity.|*Nucleic Acid Conformation[MESH]|Base Sequence[MESH]|Catalysis[MESH]|Molecular Sequence Data[MESH]|RNA, Catalytic/*metabolism[MESH] |