ISDA: 2A11

Deposition Date 2005-06-17

Release Date 2005-07-05

Last Version Date 2024-02-14

Entry Detail

PDB ID:

2A11

Keywords:

TRANSCRIPTION, TRANSLATION, HYDROLASE

Title:

Crystal Structure of Nuclease Domain of Ribonuclase III from Mycobacterium Tuberculosis

Biological Source:

Source Organism(s):

Mycobacterium tuberculosis (Taxon ID: 1773)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.10 Å

R-Value Free:

0.28

R-Value Work:

0.25

R-Value Observed:

0.28

Space Group:

P 43 21 2

Download Validation Report

Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Ribonuclease III
Chain IDs:A
Chain Length:242
Number of Molecules:1
Biological Source:Mycobacterium tuberculosis

UniProt ID:P9WH03 Pfam ID:PF14622, PF00035 EC:3.1.26.3

Ligand Molecules

Primary Citation

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

Akey, D.L, Berger, J.M.Show

Protein Sci. 14 2744 2750 (2005)

PMID: 16155207 DOI: 10.1110/ps.051665905

Abstact

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.

Legend

Protein

Chemical

Disease

Primary Citation of related structures

Abstact

Feedback Form