› 1p0d

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF ZYMOMONAS MOBILIS tRNA-GUANINE TRANSGLYCOSYLASE (TGT) CRYSTALLISED AT PH 5.5

Released:
DOI: 10.2210/pdb1p0d/pdb
PDB entry 1p0d coloured by chain, front view.
PDB entry 1p0d coloured by chain, side view.
PDB entry 1p0d coloured by chain, top view.
Source organism: Zymomonas mobilis
Primary publication:
Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug design.
Brenk R, Stubbs MT, Heine A, Reuter K, Klebe G
Chembiochem 4 1066-77 (2003)
PMID: 14523925

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 domain:

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: 42.93 KDa
Source organism: Zymomonas mobilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28720 (Residues: 2-386; Coverage: 100%)
Gene names: ZMO0363, tgt
Sequence domains: Queuine tRNA-ribosyltransferase
Structure domains: Queuine tRNA-ribosyltransferase-like

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 90.38Å b: 65.37Å c: 70.57Å
α: 90° β: 96.3° γ: 90°
R-values:
R R work R free
0.172 0.172 0.209
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Molecular recognition in chemical and biological systems.
Persch et al. (2015)
3 more

3 mentions without citation

Soaking suggests "alternative facts": Only co-crystallization discloses major ligand-induced interface rearrangements of a homodimeric tRNA-binding protein indicating a novel mode-of-inhibition.
Ehrmann et al. (2017)
2 more