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      Tertiary contacts distant from the active site prime a ribozyme for catalysis.

      Cell

      enzymology, Schistosoma mansoni, metabolism, genetics, chemistry, RNA, Catalytic, Phosphates, Nucleic Acid Conformation, Molecular Sequence Data, Models, Molecular, Hydrogen Bonding, Crystallography, X-Ray, Catalysis, Binding Sites, Base Sequence, Animals

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          Abstract

          Minimal hammerhead ribozymes have been characterized extensively by static and time-resolved crystallography as well as numerous biochemical analyses, leading to mutually contradictory mechanistic explanations for catalysis. We present the 2.2 A resolution crystal structure of a full-length Schistosoma mansoni hammerhead ribozyme that permits us to explain the structural basis for its 1000-fold catalytic enhancement. The full-length hammerhead structure reveals how tertiary interactions occurring remotely from the active site prime this ribozyme for catalysis. G-12 and G-8 are positioned consistent with their previously suggested roles in acid-base catalysis, the nucleophile is aligned with a scissile phosphate positioned proximal to the A-9 phosphate, and previously unexplained roles of other conserved nucleotides become apparent within the context of a distinctly new fold that nonetheless accommodates the previous structural studies. These interactions permit us to explain the previously irreconcilable sets of experimental results in a unified, consistent, and unambiguous manner.

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          Journal
          10.1016/j.cell.2006.06.036
          16859740

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