Disparate HDV ribozyme crystal structures represent intermediates on a rugged free-energy landscape.

ABSTRACT: The hepatitis delta virus (HDV) ribozyme is a member of the class of small, self-cleaving catalytic RNAs found in a wide range of genomes from HDV to human. Both pre- and post-catalysis (precursor and product) crystal structures of the cis-acting genomic HDV ribozyme have been determined. These structures, together with extensive solution probing, have suggested that a significant conformational change accompanies catalysis. A recent crystal structure of a trans-acting precursor, obtained at low pH and by molecular replacement from the previous product conformation, conforms to the product, raising the possibility that it represents an activated conformer past the conformational change. Here, using fluorescence resonance energy transfer (FRET), we discovered that cleavage of this ribozyme

SUBMITTER: Sripathi KN 

PROVIDER: S-EPMC4114689 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature