› 2nvo

X-ray diffraction
1.89Å resolution

Crystal structure of Deinococcus radiodurans RO (RSR) protein

Released:
DOI: 10.2210/pdb2nvo/pdb
PDB entry 2nvo coloured by chain, front view.
PDB entry 2nvo coloured by chain, side view.
PDB entry 2nvo coloured by chain, top view.
Source organism: Deinococcus radiodurans
Primary publication:
Crystal structure of Rsr, an ortholog of the antigenic Ro protein, links conformational flexibility to RNA binding activity.
Ramesh A, Savva CG, Holzenburg A, Sacchettini JC
J Biol Chem 282 14960-7 (2007)
PMID: 17392270

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-193286 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-binding protein RO60 Chain: A
Molecule details ›
Chain: A
Length: 535 amino acids
Theoretical weight: 57.85 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RUW8 (Residues: 1-531; Coverage: 100%)
Gene names: DR_1262, rsr
Sequence domains: TROVE domain
Structure domains: von Willebrand factor, type A domain

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 103.556Å b: 87.61Å c: 70.623Å
α: 90° β: 96.57° γ: 90°
R-values:
R R work R free
0.223 0.223 0.262
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Emerging roles for the Ro 60-kDa autoantigen in noncoding RNA metabolism.
Sim et al. (2011)
4 other articles

5 mentions without citation

Ro60 and Y RNAs: structure, functions, and roles in autoimmunity.
Boccitto et al. (2019)
4 more