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A recent structural study on a human RNA deaminase reveals that inositol hexakisphosphate is a cofactor of the enzyme and is essential for its editing activity.
Flock House virus protein B2 suppresses the RNA-mediated interference response by binding double-stranded RNA of almost any size or sequence. The crystal structure of this protein bound to RNA reveals a novel fold that suggests its mechanism of action.
RNase P is an ancient ribonucleoprotein (RNP) enzyme present in every living organism. Several recent reports collectively provide a structural and functional analysis of this 'simple' RNP and result in a better understanding of the apparent differences between the two types of RNase P in bacteria.