› 3h38

X-ray diffraction
2.37Å resolution

The structure of CCA-adding enzyme apo form II

Released:
DOI: 10.2210/pdb3h38/pdb
PDB entry 3h38 coloured by chain, front view.
PDB entry 3h38 coloured by chain, side view.
PDB entry 3h38 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme.
Toh Y, Takeshita D, Numata T, Fukai S, Nureki O, Tomita K
EMBO J 28 3353-65 (2009)
PMID: 19745807

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CBS domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 441 amino acids
Theoretical weight: 51.53 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZH4 (Residues: 437-863; Coverage: 50%)
Gene name: TM_0715
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2
Unit cell:
a: 173.348Å b: 50.455Å c: 69.871Å
α: 90° β: 91° γ: 90°
R-values:
R R work R free
0.214 0.211 0.266
Expression system: Escherichia coli

Quick links

Citations

6 review citations

tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization.
Betat et al. (2010)
5 more

2 mentions without citation

Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme.
Toh et al. (2009)
1 more