› 2nm3

X-ray diffraction
1.68Å resolution

Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2S)-monapterin at 1.68 angstrom resolution

Released:
DOI: 10.2210/pdb2nm3/pdb
PDB entry 2nm3 coloured by chain, front view.
PDB entry 2nm3 coloured by chain, side view.
PDB entry 2nm3 coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structural basis for the aldolase and epimerase activities of Staphylococcus aureus dihydroneopterin aldolase.
Blaszczyk J, Li Y, Gan J, Yan H, Ji X
J Mol Biol 368 161-9 (2007)
PMID: 17331536

Function and Biology Details

Reactions catalysed: 
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin = 7,8-dihydromonapterin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157538 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroneopterin aldolase Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.77 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P56740 (Residues: 1-121; Coverage: 100%)
Gene name: folB
Sequence domains: Dihydroneopterin aldolase
Structure domains: GTP Cyclohydrolase I, domain 2

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand MPU 1 x MPU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: I422
Unit cell:
a: 61.191Å b: 61.191Å c: 124.528Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 not available 0.262
Expression system: Escherichia coli

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Citations

4 review citations

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

2 mentions without citation

Structural basis for the aldolase and epimerase activities of Staphylococcus aureus dihydroneopterin aldolase.
Blaszczyk et al. (2007)
1 more