2e7y

X-ray diffraction
1.97Å resolution

High resolution structure of T. maritima tRNase Z

Released:
Source organism: Thermotoga maritima
Primary publication:
The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes.
Acta Crystallogr Sect F Struct Biol Cryst Commun 63 637-41 (2007)
PMID: 17671357

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-194650 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 32.71 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9WZW8 (Residues: 1-280; Coverage: 100%)
Gene name: TM_0864
Sequence domains: Beta-lactamase superfamily domain
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2221
Unit cell:
a: 150.299Å b: 172.694Å c: 64.886Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.249
Expression system: Escherichia coli BL21(DE3)