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X-ray diffraction
2.28Å resolution

Crystal structure of human tRNAHis guanylyltransferase (Thg1)- NaI derivative

Released:
DOI: 10.2210/pdb3otd/pdb
PDB entry 3otd coloured by chain, front view.
PDB entry 3otd coloured by chain, side view.
PDB entry 3otd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.
Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublié S
Proc Natl Acad Sci U S A 107 20305-10 (2010)
PMID: 21059936

Function and Biology Details

Reaction catalysed: 
(1a) p-tRNA(His) + ATP = A-Ppp-tRNA(His) + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192666 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable tRNA(His) guanylyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 269 amino acids
Theoretical weight: 31.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NWX6 (Residues: 30-298; Coverage: 90%)
Gene names: ICF45, THG1L
Sequence domains:
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand IOD 10 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P43212
Unit cell:
a: 140.574Å b: 140.574Å c: 80.962Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Doing it in reverse: 3'-to-5' polymerization by the Thg1 superfamily.
Jackman et al. (2012)
10 more

3 mentions without citation

tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.
Hyde et al. (2010)
2 more