Hairpin Ribozyme

This Sandbox is Reserved from September 14, 2021, through May 31, 2022, for use in the class Introduction to Biochemistry taught by User:John Means at the University of Rio Grande, Rio Grande, OH, USA. This reservation includes 5 reserved sandboxes (Sandbox Reserved 1590 through Sandbox Reserved 1594).

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Hairpin Ribozyme Overview (maybe something like 'Structure')

spinqualitylabelsall models Crystal Structure of the Hairpin Ribozyme in the catalytically-active conformation (PDB entry 1m5k) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Anything in this section will appear adjacent to the 3D structure and will be scrollable. The hairpin ribozyme is a member of a small family of RNA endonucleases that includes hammerhead, hepatitis delta, and Neurospora VS. Endonucleases are enzymes that cleave phosphodiester bonds within polynucleotide chains. This group of endonucleases cleave RNA substrates in a reversible reaction that generates a 2', 3'-cyclic phosphate and a 5'-hydroxyl termini. The hairpin ribozyme was discovered in the negative strand of the tobacco ringspot virus satellite RNA. Study of hairpin ribozyme reaction mechanisms provided early evidence that ribozymes are able to exploit a variety of strategies, just like protein enzymes. But, the hairpin ribozyme has a unique characteristic. Unlike other ribozymes, the hairpin ribozyme does not require metal ions for cleavage or ligation of substrate RNA. catalytically active

Structure

In the transition state, the hairpin ribozyme

Proteopedia Page Contributors and Editors (what is this?)

Michael Parcell, Jaime Prilusky, Michal Harel, John Means