› 2vef

X-ray diffraction
1.8Å resolution

Dihydropteroate synthase from Streptococcus pneumoniae

Released:
DOI: 10.2210/pdb2vef/pdb
PDB entry 2vef coloured by chain, front view.
PDB entry 2vef coloured by chain, side view.
PDB entry 2vef coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Dihydropteroate synthase from Streptococcus pneumoniae: structure, ligand recognition and mechanism of sulfonamide resistance.
Levy C, Minnis D, Derrick JP
Biochem J 412 379-88 (2008)
PMID: 18321242

Function and Biology Details

Reaction catalysed: 
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157834 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropteroate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 34.46 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P59655 (Residues: 1-314; Coverage: 100%)
Gene names: spr0266, sulA
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P212121
Unit cell:
a: 45.613Å b: 90.382Å c: 138.656Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.24
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Utility of the Biosynthetic Folate Pathway for Targets in Antimicrobial Discovery.
Bourne CR. (2014)
4 more

1 mention without citation

Crystal structures of Burkholderia cenocepacia dihydropteroate synthase in the apo-form and complexed with the product 7,8-dihydropteroate.
Morgan et al. (2011)