2A11

Crystal Structure of Nuclease Domain of Ribonuclase III from Mycobacterium Tuberculosis

Summary for 2A11

• Entry DOI: 10.2210/pdb2a11/pdb
• Descriptor: Ribonuclease III, CALCIUM ION (3 entities in total)
• Functional Keywords: ribonuclease; rnase iii; nuclease domain; structural genomics, psi, protein structure initiative; mycobacterium tuberculosis structural proteomics project (xmtb), transcription, translation, hydrolase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 25637.14

Authors

Akey, D.L.,Berger, J.M.,Mycobacterium Tuberculosis Structural Proteomics Project (XMTB) (deposition date: 2005-06-17, release date: 2005-07-05, Last modification date: 2024-02-14)

Primary citation

Akey, D.L.,Berger, J.M.
Structure of the nuclease domain of ribonuclease III from M. tuberculosis at 2.1 A
Protein Sci., 14:2744-2750, 2005

PubMed Abstract: 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.

PubMed: 16155207
DOI: 10.1110/ps.051665905

Experimental method

X-RAY DIFFRACTION (2.1 Å)