1rlv

X-ray diffraction
3Å resolution

Crystal structure of a dimeric Archaeal Splicing Endonuclease

Released:
Source organism: Archaeoglobus fulgidus
Primary publication:
Crystal structure of a dimeric archaeal splicing endonuclease.
J. Mol. Biol. 302 639-48 (2000)
PMID: 10986124

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

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA-splicing endonuclease Chains: A, B
Molecule details ›
Chains: A, B
Length: 305 amino acids
Theoretical weight: 36 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O29362 (Residues: 1-305; Coverage: 100%)
Gene names: AF_0900, endA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P43212
Unit cell:
a: 126.817Å b: 126.817Å c: 130.231Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.276
Expression system: Escherichia coli