Abstract:
: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 pKa that 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.
journal_name
PLoS Bioljournal_title
PLoS biologyauthors
Chi YI,Martick M,Lares M,Kim R,Scott WG,Kim SHdoi
10.1371/journal.pbio.0060234subject
Has Abstractpub_date
2008-09-30 00:00:00pages
e234issue
9eissn
1544-9173issn
1545-7885pii
08-PLBI-RA-1371journal_volume
6pub_type
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