› 1ylh

X-ray diffraction
1.7Å resolution

Crystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and Pyruvate

Released:
DOI: 10.2210/pdb1ylh/pdb
PDB entry 1ylh coloured by chain, front view.
PDB entry 1ylh coloured by chain, side view.
PDB entry 1ylh coloured by chain, top view.
Source organism: Actinobacillus succinogenes
Primary publication:
Structure of PEP carboxykinase from the succinate-producing Actinobacillus succinogenes: a new conserved active-site motif.
Leduc YA, Prasad L, Laivenieks M, Zeikus JG, Delbaere LT
Acta Crystallogr D Biol Crystallogr 61 903-12 (2005)
PMID: 15983413

Function and Biology Details

Reaction catalysed: 
ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108135 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxykinase (ATP) Chain: A
Molecule details ›
Chain: A
Length: 560 amino acids
Theoretical weight: 61.9 KDa
Source organism: Actinobacillus succinogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: A6VKV4 (Residues: 1-538; Coverage: 100%)
Gene names: Asuc_0221, pckA
Sequence domains: Phosphoenolpyruvate carboxykinase
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand MN 1 x MN
Ligand PO4 2 x PO4
Ligand DT3 1 x DT3
Ligand BME 2 x BME
Ligand PYR 1 x PYR
Ligand FMT 3 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P21
Unit cell:
a: 56.737Å b: 55.089Å c: 90.077Å
α: 90° β: 106.17° γ: 90°
R-values:
R R work R free
0.195 0.19 0.215
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Metabolic engineering of carbon and redox flow in the production of small organic acids.
Thakker et al. (2015)
1 more