› 4em4

X-ray diffraction
1.82Å resolution

Crystal Structure of Staphylococcus aureus bound with the covalent inhibitor Pethyl-VS-CoA

Released:
DOI: 10.2210/pdb4em4/pdb
PDB entry 4em4 coloured by chain, front view.
PDB entry 4em4 coloured by chain, side view.
PDB entry 4em4 coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus USA300
Primary publication:
Turnover-dependent covalent inactivation of Staphylococcus aureus coenzyme A-disulfide reductase by coenzyme A-mimetics: mechanistic and structural insights.
Wallace BD, Edwards JS, Wallen JR, Moolman WJ, van der Westhuyzen R, Strauss E, Redinbo MR, Claiborne A
Biochemistry 51 7699-711 (2012)
PMID: 22954034

Function and Biology Details

Reaction catalysed: 
2 CoA + NADP(+) = CoA-disulfide + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coenzyme A disulfide reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 437 amino acids
Theoretical weight: 49.22 KDa
Source organism: Staphylococcus aureus subsp. aureus USA300
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2FIA5 (Residues: 2-438; Coverage: 100%)
Gene names: SAUSA300_0873, cdr
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand CA8 2 x CA8
2 bound ligands:
Ligand MG 3 x MG
Ligand CL 7 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 76.144Å b: 64.909Å c: 94.442Å
α: 90° β: 104.62° γ: 90°
R-values:
R R work R free
0.156 0.154 0.202
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Coping with inevitable accidents in metabolism.
Danchin A. (2017)
2 other articles

1 mention without citation

Turnover-dependent covalent inactivation of Staphylococcus aureus coenzyme A-disulfide reductase by coenzyme A-mimetics: mechanistic and structural insights.
Wallace et al. (2012)