› 1zvw

X-ray diffraction
2.3Å resolution

The Crystal Structure of TrpD (Rv2192c) from Mycobacterium tuberculosis in Complex with PRPP and Magnesium

Released:
DOI: 10.2210/pdb1zvw/pdb
PDB entry 1zvw coloured by chain, front view.
PDB entry 1zvw coloured by chain, side view.
PDB entry 1zvw coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate.
Lee CE, Goodfellow C, Javid-Majd F, Baker EN, Shaun Lott J
J Mol Biol 355 784-97 (2006)
PMID: 16337227

Function and Biology Details

Reaction catalysed: 
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anthranilate phosphoribosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 378 amino acids
Theoretical weight: 39.22 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WFX5 (Residues: 1-370; Coverage: 100%)
Gene names: MTCY190.03c, Rv2192c, trpD
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand PRP 1 x PRP
Ligand BEN 1 x BEN
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 80.417Å b: 82.076Å c: 118.873Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.255
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.
Hove-Jensen et al. (2017)
7 more

2 mentions without citation

Structure, mechanism and inhibition of anthranilate phosphoribosyltransferase.
Scully et al. (2023)
1 more