2ffl
Crystal Structure of Dicer from Giardia intestinalis
OverviewOverview
The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.
About this StructureAbout this Structure
2FFL is a Single protein structure of sequence from Giardia intestinalis. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for double-stranded RNA processing by Dicer., Macrae IJ, Zhou K, Li F, Repic A, Brooks AN, Cande WZ, Adams PD, Doudna JA, Science. 2006 Jan 13;311(5758):195-8. PMID:16410517 Page seeded by OCA on Sun May 4 03:50:20 2008