1mme
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THE CRYSTAL STRUCTURE OF AN ALL-RNA HAMMERHEAD RIBOZYME: A PROPOSED MECHANISM FOR RNA CATALYTIC CLEAVAGE
OverviewOverview
We have solved the crystal structure of an all-RNA hammerhead ribozyme, having a single 2'-O-methyl cytosine incorporated at the active site to, prevent cleavage. The conditions used differ from those in another recent, solution in four significant ways: first, it is an all-RNA ribozyme rather, than a DNA-RNA hybrid; second, the connectivity of the ribozyme backbone, strands is different; third, the crystals were grown in the presence of a, much lower concentration of salt; and fourth, the crystal packing scheme, is very different. Nevertheless, the three-dimensional structure of the, all-RNA hammerhead ribozyme is similar to the previous structure. Five, potential Mg(II)-binding sites are identified, including one positioned, near the ribozyme catalytic pocket. Upon this basis, as well as upon, comparisons with the metal-binding sites in the structurally homologous, uridine turn of tRNAPhe, we propose a mechanism for RNA catalytic, cleavage.
About this StructureAbout this Structure
1MME is a Protein complex structure of sequences from [1]. The following page contains interesting information on the relation of 1MME with [Self-splicing RNA]. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA catalytic cleavage., Scott WG, Finch JT, Klug A, Cell. 1995 Jun 30;81(7):991-1002. PMID:7541315
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