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Structure of the nuclease domain of ribonuclease III from M. tuberculosis at 2.1 Å
Author(s) -
Akey David L.,
Berger James M.
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051665905
Subject(s) - rnase p , rnase h , rna , ribonuclease , nuclease , biology , ribonuclease iii , genetics , microbiology and biotechnology , dna , gene , rna interference
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.