› 2gn4

X-ray diffraction
1.9Å resolution

Crystal structure of UDP-GlcNAc inverting 4,6-dehydratase in complex with NADPH and UDP-GlcNAc

Released:
DOI: 10.2210/pdb2gn4/pdb
Model geometry
Fit model/data
PDB entry 2gn4 coloured by chain, front view.
PDB entry 2gn4 coloured by chain, side view.
PDB entry 2gn4 coloured by chain, top view.
Source organism: Helicobacter pylori
Primary publication:
Structural studies of FlaA1 from Helicobacter pylori reveal the mechanism for inverting 4,6-dehydratase activity.
Ishiyama N, Creuzenet C, Miller WL, Demendi M, Anderson EM, Harauz G, Lam JS, Berghuis AM
J Biol Chem 281 24489-95 (2006)
PMID: 16651261

Function and Biology Details

Reaction catalysed: 
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 4,6-dehydratase (inverting) Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 38.72 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: O25511 (Residues: 1-333; Coverage: 100%)
Gene names: HP_0840, flaA1, pseB
Sequence domains: Polysaccharide biosynthesis protein
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
2 bound ligands:
Ligand UD1 2 x UD1
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P63
Unit cell:
a: 111.357Å b: 111.357Å c: 107.991Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 0.229
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Review: Lipopolysaccharide biosynthesis in Pseudomonas aeruginosa.
King et al. (2009)
3 more

6 mentions without citation

Nucleotide sugar dehydratases: Structure, mechanism, substrate specificity, and application potential.
Vogel et al. (2022)
5 more