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:
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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