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Folding and catalysis by the hairpin ribozyme
Author(s) -
Lilley David M.J
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00544-x
Subject(s) - hairpin ribozyme , vs ribozyme , ribozyme , phosphodiester bond , antiparallel (mathematics) , stacking , chemistry , crystallography , mammalian cpeb3 ribozyme , stereochemistry , biophysics , physics , biochemistry , biology , rna , organic chemistry , quantum mechanics , magnetic field , gene
The 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 S N 2 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.