› 3bl3

X-ray diffraction
2.25Å resolution

Function and Biology Details

Reaction catalysed: 
Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Queuine tRNA-ribosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 386 amino acids
Theoretical weight: 42.87 KDa
Source organism: Zymomonas mobilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P28720 (Residues: 1-386; Coverage: 100%)
Gene names: ZMO0363, tgt
Sequence domains: Queuine tRNA-ribosyltransferase
Structure domains: Queuine tRNA-ribosyltransferase-like

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 90.686Å b: 64.774Å c: 70.4Å
α: 90° β: 95.94° γ: 90°
R-values:
R R work R free
0.187 0.187 0.227
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The queuine micronutrient: charting a course from microbe to man.
Fergus et al. (2015)
1 more

1 mention without citation

Investigation of specificity determinants in bacterial tRNA-guanine transglycosylase reveals queuine, the substrate of its eucaryotic counterpart, as inhibitor.
Biela et al. (2013)