› 4hnu

X-ray diffraction
3Å resolution

crystal structure of K442E mutant of S. aureus Pyruvate carboxylase

Released:
DOI: 10.2210/pdb4hnu/pdb
PDB entry 4hnu coloured by chain, front view.
PDB entry 4hnu coloured by chain, side view.
PDB entry 4hnu coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Characterizing the importance of the biotin carboxylase domain dimer for Staphylococcus aureus pyruvate carboxylase catalysis.
Yu LP, Chou CY, Choi PH, Tong L
Biochemistry 52 488-96 (2013)
PMID: 23286247

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate carboxylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 1173 amino acids
Theoretical weight: 131.17 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3JRU9 (Residues: 1-1150; Coverage: 100%)
Gene names: SAV1114, pycA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand BTI 1 x BTI
2 bound ligands:
Ligand ADP 1 x ADP
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 96.569Å b: 258.52Å c: 126.898Å
α: 90° β: 109.6° γ: 90°
R-values:
R R work R free
0.197 0.194 0.262
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Allosteric modulation of protein oligomerization: an emerging approach to drug design.
Gabizon et al. (2014)
7 other articles

1 mention without citation

Characterizing the importance of the biotin carboxylase domain dimer for Staphylococcus aureus pyruvate carboxylase catalysis.
Yu et al. (2013)