The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA catalytic cleavage
Article Abstract:
The crystal structure of an all-RNA hammerhead ribozyme is determined and found to have a single 2'-O-methyl cytosine at the active site to avoid cleavage. The discovery that RNA can act as an enzyme has stimulated research to determine the mechanisms of RNA catalysis. Though the conditions are different in respect of the method of growing crystals and connectivity of the ribozyme backbone, the structure is comparable to previous ones. A mechanism for divalent metal ion-mediated RNA catalytic cleavage has been proposed based on the homologous metal-binding sites in the tRNA crystals.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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The structural basis of hammerhead ribozyme self-cleavage
Article Abstract:
Research was conducted to study structural concerns associated with the cleavage site of the hammerhead ribozyme during self-cleavage. A cyclic phosphate diester was utilized to model scissile phosphate. Results showed that the ground RNA structures did not reveal the cleavage mechanism and indicated that the phosphate conformation of the kinetically trapped intermediate structure was close to that inhabited by the transition form of the cleavage reaction.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Tertiary contacts distant from the active site prime a ribozyme for catalysis
Article Abstract:
The 2.2 Angstrom resolution crystal structure of a full-length Schistosoma mansoni hammerhead ribozyme is used to explain the structural basis for its 1000-fold catalytic enhancement. The full-length hammerhead structure reveals how tertiary interactions occurring remotely from active site prime this ribozyme for catalysis.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
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