› 1ou5

X-ray diffraction
3.4Å resolution

Crystal structure of human CCA-adding enzyme

Released:
DOI: 10.2210/pdb1ou5/pdb
PDB entry 1ou5 coloured by chain, front view.
PDB entry 1ou5 coloured by chain, side view.
PDB entry 1ou5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization.
Augustin MA, Reichert AS, Betat H, Huber R, Mörl M, Steegborn C
J Mol Biol 328 985-94 (2003)
PMID: 12729736

Function and Biology Details

Reaction catalysed: 
(1a) a tRNA precursor + CTP = a tRNA with a 3' cytidine end + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188688 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CCA tRNA nucleotidyltransferase 1, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 448 amino acids
Theoretical weight: 51.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96Q11 (Residues: 29-434; Coverage: 94%)
Gene names: CGI-47, TRNT1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 102.52Å b: 102.52Å c: 206.658Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.282 0.278 0.318
Expression system: Escherichia coli

Quick links

Citations

10 review citations

RNA-specific ribonucleotidyl transferases.
Martin et al. (2007)
9 more

9 mentions without citation

Biochemistry of Autoinflammatory Diseases: Catalyzing Monogenic Disease.
Beck et al. (2019)
8 more