› 1w54

X-ray diffraction
2.2Å resolution

Stepwise introduction of a zinc binding site into Porphobilinogen synthase from Pseudomonas aeruginosa (mutation D139C)

Released:
DOI: 10.2210/pdb1w54/pdb
PDB entry 1w54 coloured by chain, front view.
PDB entry 1w54 coloured by chain, side view.
PDB entry 1w54 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Tracking the evolution of porphobilinogen synthase metal dependence in vitro.
Frère F, Reents H, Schubert WD, Heinz DW, Jahn D
J Mol Biol 345 1059-70 (2005)
PMID: 15644204

Function and Biology Details

Reaction catalysed: 
2 5-aminolevulinate = porphobilinogen + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176810 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-aminolevulinic acid dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.05 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q59643 (Residues: 1-337; Coverage: 100%)
Gene names: PA5243, hemB
Sequence domains: Delta-aminolevulinic acid dehydratase
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand FMT 2 x FMT
Ligand K 2 x K
Ligand MG 2 x MG
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P4212
Unit cell:
a: 125.231Å b: 125.232Å c: 86.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.154 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The biochemistry of heme biosynthesis.
Heinemann et al. (2008)
3 more