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PROTEIN STRUCTURE REPORT

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

Department of Molecular and Cellular Biology, University of California (U.C.), Berkeley, Berkeley, California 94720, USA

(RECEIVED June 29, 2005; FINAL REVISION June 29, 2005; ACCEPTED July 5, 2005)

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.

Keywords: RNaseIII; dsRNA; RNA processing; RNA interference; enzymes; protein–nucleic acid interactions; crystallography; genomics—structural

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051665905.

Reprint requests to: James M. Berger, Department of Molecular and Cellular Biology, University of California, Berkeley, Berkeley, CA 94720, USA; e-mail: jmberger{at}berkeley.edu; fax: (510) 643-9290.

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