› 6mgi

X-ray diffraction
2.99Å resolution

Photosynthetic phosphoenolpyruvate carboxylase isoenzyme from maize complexed with the allosteric activator glucose-6-phosphate in its allosteric site

Released:
DOI: 10.2210/pdb6mgi/pdb
PDB entry 6mgi coloured by chain, front view.
PDB entry 6mgi coloured by chain, side view.
PDB entry 6mgi coloured by chain, top view.
Source organism: Zea mays
Primary publication:
Structural and biochemical evidence of the glucose 6-phosphate-allosteric site of maize C4-phosphoenolpyruvate carboxylase: its importance in the overall enzyme kinetics.
Muñoz-Clares RA, González-Segura L, Juárez-Díaz JA, Mújica-Jiménez C
Biochem J 477 2095-2114 (2020)
PMID: 32459324

Function and Biology Details

Reaction catalysed: 
Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138156 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxylase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 970 amino acids
Theoretical weight: 109.48 KDa
Source organism: Zea mays
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04711 (Residues: 1-970; Coverage: 100%)
Gene names: PEP1, PPC
Sequence domains: Phosphoenolpyruvate carboxylase

Ligands and Environments

5 bound ligands:
Ligand GLY 2 x GLY
Ligand G6P 2 x G6P
Ligand EDO 6 x EDO
Ligand PGA 2 x PGA
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 152.087Å b: 170.679Å c: 244.622Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.244
Expression system: Escherichia coli BL21

Quick links

Citations

1 mention without citation

Multiple conformations in solution of the maize C4-phosphoenolpyruvate carboxylase isozyme.
Barreda-Huerta et al. (2021)