› 2y4r

X-ray diffraction
1.75Å resolution

CRYSTAL STRUCTURE OF 4-AMINO-4-DEOXYCHORISMATE LYASE FROM PSEUDOMONAS AERUGINOSA

Released:
DOI: 10.2210/pdb2y4r/pdb
PDB entry 2y4r coloured by chain, front view.
PDB entry 2y4r coloured by chain, side view.
PDB entry 2y4r coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Pseudomonas aeruginosa 4-amino-4-deoxychorismate lyase: spatial conservation of an active site tyrosine and classification of two types of enzyme.
O'Rourke PE, Eadsforth TC, Fyfe PK, Shepherd SM, Hunter WN
PLoS One 6 e24158 (2011)
PMID: 21935381

Function and Biology Details

Reaction catalysed: 
4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
aminodeoxychorismate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 292 amino acids
Theoretical weight: 32.34 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HZN6 (Residues: 1-271; Coverage: 100%)
Gene names: PA2964, pabC
Sequence domains: Amino-transferase class IV
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
6 bound ligands:
Ligand PG4 5 x PG4
Ligand CL 3 x CL
Ligand SO4 2 x SO4
Ligand EDO 3 x EDO
Ligand PEG 3 x PEG
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 40.813Å b: 66.817Å c: 202.688Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.215
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Strategic Moves of "Superbugs" Against Available Chemical Scaffolds: Signaling, Regulation, and Challenges.
Baral et al. (2020)
4 other articles

4 mentions without citation

Pseudomonas aeruginosa 4-amino-4-deoxychorismate lyase: spatial conservation of an active site tyrosine and classification of two types of enzyme.
O'Rourke et al. (2011)
3 more