Key result
The crystal structure of the nuclease domain of RNase III from Mycobacterium tuberculosis reveals an additional metal ion near the catalytic site and conserved secondary structural elements.
The crystal structure of M. tuberculosis RNase III nuclease domain reveals novel features including an additional metal ion near the catalytic site, providing insights into dsRNA recognition.
RNase III enzymes are a highly conserved family of proteins that specifically cleave double-stranded (ds)RNA. These proteins are involved in a diverse group of functions, including ribosomal RNA processing, mRNA maturation and decay, snRNA and snoRNA processing, and RNA interference. Here we report the crystal structure of the nuclease domain of RNase III from the pathogen Mycobacterium tuberculosis. Although globally similar to other RNase III folds, this structure has some features not observed in previously reported models. These include the presence of an additional metal ion near the catalytic site, as well as conserved secondary structural elements that are proposed to have functional roles in the recognition of dsRNAs.
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Akey et al. (2005) studied this question. The crystal structure of the nuclease domain of RNase III from Mycobacterium tuberculosis reveals an additional metal ion near the catalytic site and conserved secondary structural elements.
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