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Catalytic form of RNase III for dsRNA processing. The crystal structure of dimeric Aquifex aeolicus RNase III in complex with dsRNA (Aa-RNase IIIodsRNA) was determined at 1.7-Å resolution (PDB: 2NUG). The highly symmetric structure reveals that the dimerization of the two catalytic domains (RIIIDs) is essential for the formation of two RNA cleavage sites precisely arranged to produce the characteristic 2-nucleotide 3´ overhang of RNase III products. The two RIIIDs are shown as molecular surface; the two dsRNA-binding domains are illustrated as ribbon diagrams (helices as spirals, strands as arrows, and loops as pipes). The two subunits are colored in cyan and orange, respectively. The Mg ions are indicated with black spheres; the two cleaved RNA strands are shown as tube-and-stick models in blue and red, respectively. (Jianhua Gan, Gary Shaw et al. Mol. Microbiol. 67:143-154, 2008. PubMed: 18047582).