› 4hnv

X-ray diffraction
2.8Å resolution

Crystal structure of R54E mutant of S. aureus Pyruvate carboxylase

Released:
DOI: 10.2210/pdb4hnv/pdb
PDB entry 4hnv coloured by chain, front view.
PDB entry 4hnv coloured by chain, side view.
PDB entry 4hnv 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:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 96.434Å b: 256.742Å c: 127.045Å
α: 90° β: 109.33° 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)