2a11
Crystal Structure of Nuclease Domain of Ribonuclase III from Mycobacterium TuberculosisCrystal Structure of Nuclease Domain of Ribonuclase III from Mycobacterium Tuberculosis
Structural highlights
Function[RNC_MYCTU] Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism (By similarity).[HAMAP-Rule:MF_00104] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRNase 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. Structure of the nuclease domain of ribonuclease III from M. tuberculosis at 2.1 A.,Akey DL, Berger JM Protein Sci. 2005 Oct;14(10):2744-50. Epub 2005 Sep 9. PMID:16155207[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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