4hb7

X-ray diffraction
1.95Å resolution

The Structure of Dihydropteroate Synthase from Staphylococcus aureus subsp. aureus Mu50.

Released:
Entry authors: Cuff ME, Holowicki J, Jedrzejczak R, Terwilliger TC, Rubin EJ, Guinn K, Baker D, Ioerger TR, Sacchettini JC, Joachimiak A, Midwest Center for Structural Genomics (MCSG), Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors (MTBI)

Function and Biology Details

Reaction catalysed:
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropteroate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 270 amino acids
Theoretical weight: 29.84 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P64141 (Residues: 1-267; Coverage: 100%)
Gene names: SAV0514, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 90.584Å b: 77.301Å c: 90.546Å
α: 90° β: 99.75° γ: 90°
R-values:
R R work R free
0.164 0.162 0.206
Expression system: Escherichia coli BL21(DE3)