› 2y5s

X-ray diffraction
1.95Å resolution

Crystal structure of Burkholderia cenocepacia dihydropteroate synthase complexed with 7,8-dihydropteroate.

Released:
DOI: 10.2210/pdb2y5s/pdb
PDB entry 2y5s coloured by chain, front view.
PDB entry 2y5s coloured by chain, side view.
PDB entry 2y5s coloured by chain, top view.
Source organism: Burkholderia cenocepacia
Primary publication:
Crystal structures of Burkholderia cenocepacia dihydropteroate synthase in the apo-form and complexed with the product 7,8-dihydropteroate.
Morgan RE, Batot GO, Dement JM, Rao VA, Eadsforth TC, Hunter WN
BMC Struct Biol 11 21 (2011)
PMID: 21554707

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropteroate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 31 KDa
Source organism: Burkholderia cenocepacia
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B4E5F5 (Residues: 1-292; Coverage: 100%)
Gene names: BCAL1268, dhpS, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

3 bound ligands:
Ligand 78H 2 x 78H
Ligand CL 2 x CL
Ligand EDO 16 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 73.662Å b: 86.92Å c: 88.795Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.176 0.211
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

2 mentions 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)
1 more