› 2cg8

X-ray diffraction
2.9Å resolution

The bifunctional dihydroneopterin aldolase 6-hydroxymethyl-7,8- dihydropterin synthase from Streptococcus pneumoniae

Released:
DOI: 10.2210/pdb2cg8/pdb
PDB entry 2cg8 coloured by chain, front view.
PDB entry 2cg8 coloured by chain, side view.
PDB entry 2cg8 coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Crystal structure of the bifunctional dihydroneopterin aldolase/6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Streptococcus pneumoniae.
Garçon A, Levy C, Derrick JP
J Mol Biol 360 644-53 (2006)
PMID: 16781731

Function and Biology Details

Reactions catalysed: 
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157835 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional folate synthesis protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 270 amino acids
Theoretical weight: 31.13 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P59657 (Residues: 1-270; Coverage: 100%)
Gene names: spr0269, sulD
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P41212
Unit cell:
a: 149.44Å b: 149.44Å c: 238.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.215 0.241
Expression system: Escherichia coli

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Citations

5 review citations

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