Structure of the nuclease domain of ribonuclease III from M. tuberculosis at 2.1 Å

David L. Akey, James M. Berger

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)2744-2750
Number of pages7
JournalProtein Science
Issue number10
StatePublished - Oct 2005
Externally publishedYes


  • Crystallography
  • Enzymes
  • Genomics-structural
  • Protein-nucleic acid interactions
  • RNA interference
  • RNA processing
  • RNaseIII
  • dsRNA

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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