Journal
PROTEIN SCIENCE
Volume 14, Issue 10, Pages 2744-2750Publisher
WILEY
DOI: 10.1110/ps.051665905
Keywords
RNaseIII; dsRNA; RNA processing; RNA interference; enzymes; protein-nucleic acid interactions; crystallography; genomics-structural
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Funding
- NIGMS NIH HHS [P50 GM62410, P50 GM062410] Funding Source: Medline
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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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