› 4n5v

X-ray diffraction
1.9Å resolution

Alternative substrates of Mycobacterium tuberculosis anthranilate phosphoribosyl transferase

Released:
DOI: 10.2210/pdb4n5v/pdb
PDB entry 4n5v coloured by chain, front view.
PDB entry 4n5v coloured by chain, side view.
PDB entry 4n5v coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis.
Cookson TV, Castell A, Bulloch EM, Evans GL, Short FL, Baker EN, Lott JS, Parker EJ
Biochem J 461 87-98 (2014)
PMID: 24712732

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161439 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anthranilate phosphoribosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 378 amino acids
Theoretical weight: 38.79 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WFX5 (Residues: 1-370; Coverage: 100%)
Gene names: MTCY190.03c, Rv2192c, trpD
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand PRP 2 x PRP
Ligand MG 4 x MG
Ligand FA0 4 x FA0
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 79.595Å b: 92.542Å c: 121.063Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.
Parthasarathy et al. (2018)
1 more

4 mentions without citation

The tryptophan biosynthetic pathway is essential for Mycobacterium tuberculosis to cause disease.
Lott JS. (2020)
3 more