› 4b5x

X-ray diffraction
1.8Å resolution

Crystal structures of divalent metal dependent pyruvate aldolase (HpaI), mutant D42A

Released:
DOI: 10.2210/pdb4b5x/pdb
PDB entry 4b5x coloured by chain, front view.
PDB entry 4b5x coloured by chain, side view.
PDB entry 4b5x coloured by chain, top view.
Source organism: Escherichia coli ATCC 8739
Primary publication:
Crystal structure of reaction intermediates in pyruvate class II aldolase: substrate cleavage, enolate stabilization, and substrate specificity.
Coincon M, Wang W, Sygusch J, Seah SY
J Biol Chem 287 36208-21 (2012)
PMID: 22908224

Function and Biology Details

Reaction catalysed: 
4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-2-oxo-heptane-1,7-dioate aldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 28.05 KDa
Source organism: Escherichia coli ATCC 8739
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B1IS70 (Residues: 1-262; Coverage: 100%)
Gene names: EcolC_3707, hpaI, hpcH
Sequence domains: HpcH/HpaI aldolase/citrate lyase family
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

2 bound ligands:
Ligand PO4 8 x PO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS
Spacegroup: P213
Unit cell:
a: 151.17Å b: 151.17Å c: 151.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.165 0.193
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

DHAP-dependent aldolases from (hyper)thermophiles: biochemistry and applications.
Falcicchio et al. (2014)
8 other articles

1 mention without citation

Crystal structure of reaction intermediates in pyruvate class II aldolase: substrate cleavage, enolate stabilization, and substrate specificity.
Coincon et al. (2012)