3iey

X-ray diffraction
2.11Å resolution

Crystal Structure of the functional Nanoarchaeum equitans tRNA splicing endonuclease

Released:

Function and Biology Details

Reaction catalysed:
PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
PDBe Complex ID:
PDB-CPX-181081 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
tRNA-splicing endonuclease Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 18.32 KDa
Source organism: Nanoarchaeum equitans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q74MP4 (Residues: 1-154; Coverage: 100%)
Gene names: NEQ205, endA
Sequence domains:
Structure domains: Trna Endonuclease; Chain: A, domain 1
tRNA intron endonuclease catalytic domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 153 amino acids
Theoretical weight: 18.45 KDa
Source organism: Nanoarchaeum equitans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q74MS9 (Residues: 1-153; Coverage: 100%)
Gene name: NEQ261
Sequence domains: tRNA intron endonuclease, catalytic C-terminal domain
Structure domains: Trna Endonuclease; Chain: A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I41
Unit cell:
a: 124.102Å b: 124.102Å c: 69.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.232 0.259
Expression system: Escherichia coli