A. 
Click on the image to see the
full-size view, or watch a
movie
of the model rotation (1.14MB).
(Download QuickTime)
|
B. 
Click on the image to see the
full-size view, or watch a
movie of the
self-cleavage
reaction (1.08MB).
(Download QuickTime)
|
|
- Co-crystal structure
of the genomic HDV ribozyme bound to the U1A-RBD protein
(a small, basic protein that facilitates crystallization and
does not affect ribozyme activity). The 2.3-Å structure
shows that the compact catalytic core comprises five helical
segments connected as an intricate nested double pseudoknot.
The gold ball represents the catalytically critical divalent
metal ion at the active site.
- Comparison of crystal structures of the ribozyme in the
pre- and post-cleavage states (panes 1 and 2, respectively)
reveals a significant conformational change in the RNA after
cleavage and that a catalytically critical divalent metal
ion from the active site is ejected.
References:
Ke, A., Zhou, K., Ding, F., Cate, J.H.D. and Doudna, J.A. (2004)
A conformational switch controls hepatitis delta virus ribozyme catalysis. Nature, 429, 201-205.
(348KB PDF)
Ferré-D'Amaré, A.R., Zhou, K. and Doudna J.A. (1998)
Crystal structure of a hepatitis delta virus ribozyme. Nature 395, 567-574.
(684KB PDF)
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