Capturing hammerhead ribozyme structures in action by modulating general base catalysis
| Autor: | Monika Martick, Sung-Hou Kim, William G. Scott, Rosalind Kim, Young In Chi, Monica Lares |
|---|---|
| Přispěvatelé: | Joyce, Gerald F |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Hammerhead ribozyme
Stereochemistry QH301-705.5 Nepovirus Molecular Sequence Data Crystallography X-Ray Biochemistry Medical and Health Sciences Catalysis General Biochemistry Genetics and Molecular Biology Substrate Specificity Enzyme Stability Genetics RNA Catalytic Nucleic acid structure Biology (General) Catalytic Crystallography Molecular Structure Base Sequence Agricultural and Veterinary Sciences General Immunology and Microbiology biology General Neuroscience Ribozyme Leaving group RNA Biological Sciences biology.organism_classification Enzyme structure Infectious Diseases Synopsis X-Ray biology.protein Nucleic Acid Conformation General Agricultural and Biological Sciences Hairpin ribozyme VS ribozyme Developmental Biology |
| Zdroj: | PLoS Biology, Vol 6, Iss 9, p e234 (2008) PLoS biology, vol 6, iss 9 Chi, YI; Martick, M; Lares, M; Kim, R; Scott, WG; & Kim, SH. (2008). Capturing hammerhead ribozyme structures in action by modulating general base catalysis. PLoS Biology, 6(9), 2060-2068. doi: 10.1371/journal.pbio.0060234. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/173776dq PLoS Biology |
| ISSN: | 1545-7885 1544-9173 |
| DOI: | 10.1371/journal.pbio.0060234. |
| Popis: | We have obtained precatalytic (enzyme-substrate complex) and postcatalytic (enzyme-product complex) crystal structures of an active full-length hammerhead RNA that cleaves in the crystal. Using the natural satellite tobacco ringspot virus hammerhead RNA sequence, the self-cleavage reaction was modulated by substituting the general base of the ribozyme, G12, with A12, a purine variant with a much lower pKathat does not significantly perturb the ribozyme's atomic structure. The active, but slowly cleaving, ribozyme thus permitted isolation of enzyme-substrate and enzyme-product complexes without modifying the nucleophile or leaving group of the cleavage reaction, nor any other aspect of the substrate. The predissociation enzyme-product complex structure reveals RNA and metal ion interactions potentially relevant to transition-state stabilization that are absent in precatalytic structures. © 2008 Chi et al. |
| Databáze: | OpenAIRE |
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