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Capturing the structure of a catalytic RNA intermediate: the hammerhead ribozyme
W G Scott1, J B Murray, J R Arnold
1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, England.
Science (New York, N.Y.)
|December 20, 1996
Summary
The crystal structure of hammerhead ribozyme was solved, revealing its active fold. Divalent metal ions induce conformational changes at the active site, facilitating self-cleavage.
Area of Science:
- Biochemistry
- Structural Biology
- RNA catalysis
Background:
- Hammerhead ribozymes are crucial RNA enzymes capable of self-cleavage.
- Understanding their structure-function relationship is key to RNA biology.
Purpose of the Study:
- To determine the crystal structure of an unmodified hammerhead ribozyme.
- To investigate the conformational changes induced by divalent metal ions during catalysis.
Main Methods:
- X-ray crystallography was used to solve the hammerhead ribozyme structure.
- Cryo-trapping at active pH captured a catalytic intermediate.
Main Results:
- The biologically active fold of the unmodified ribozyme was elucidated.
- Divalent cations were shown to bind to the cleavage-site phosphate, forming a conformational intermediate.
- Conformational changes are localized to the active site, approaching the transition state.
Conclusions:
- The hammerhead ribozyme adopts a conserved fold across different modifications.
- Metal ion binding and subsequent conformational changes are critical for hammerhead ribozyme catalysis.
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