› 1f3e

X-ray diffraction
1.85Å resolution

A NEW TARGET FOR SHIGELLOSIS: RATIONAL DESIGN AND CRYSTALLOGRAPHIC STUDIES OF INHIBITORS OF TRNA-GUANINE TRANSGLYCOSYLASE

Released:
DOI: 10.2210/pdb1f3e/pdb
PDB entry 1f3e coloured by chain, front view.
PDB entry 1f3e coloured by chain, side view.
PDB entry 1f3e coloured by chain, top view.
Source organism: Zymomonas mobilis
Primary publication:
A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase.
Grädler U, Gerber HD, Goodenough-Lashua DM, Garcia GA, Ficner R, Reuter K, Stubbs MT, Klebe G
J Mol Biol 306 455-67 (2001)
PMID: 11178905

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
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 DPZ 1 x DPZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 90.67Å b: 64.94Å c: 71.05Å
α: 90° β: 96.61° γ: 90°
R-values:
R R work R free
0.195 0.195 0.238
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Virtual screening of chemical libraries.
Shoichet BK. (2004)
9 more

1 mention without citation

The role of aspartic acid 143 in E. coli tRNA-guanine transglycosylase: insights from mutagenesis studies and computational modeling.
Todorov et al. (2005)