› 3a9g

X-ray diffraction
2.39Å resolution

Crystal Structure of PQQ-dependent sugar dehydrogenase apo-form

Released:
DOI: 10.2210/pdb3a9g/pdb
PDB entry 3a9g coloured by chain, front view.
PDB entry 3a9g coloured by chain, side view.
PDB entry 3a9g coloured by chain, top view.
Source organism: Pyrobaculum aerophilum
Primary publication:
Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum.
Sakuraba H, Yokono K, Yoneda K, Watanabe A, Asada Y, Satomura T, Yabutani T, Motonaka J, Ohshima T
Arch Biochem Biophys 502 81-8 (2010)
PMID: 20692227

Function and Biology Details

Reaction catalysed: 
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187408 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glucose/Sorbosone dehydrogenase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 354 amino acids
Theoretical weight: 38.37 KDa
Source organism: Pyrobaculum aerophilum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8ZUN8 (Residues: 18-371; Coverage: 95%)
Gene name: PAE2689
Sequence domains: Glucose / Sorbosone dehydrogenase
Structure domains: TolB, C-terminal domain

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: I4122
Unit cell:
a: 177.74Å b: 177.74Å c: 89.937Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Lanthanides: New life metals?
Chistoserdova L. (2016)
1 more

2 mentions without citation

Discovery of a eukaryotic pyrroloquinoline quinone-dependent oxidoreductase belonging to a new auxiliary activity family in the database of carbohydrate-active enzymes.
Matsumura et al. (2014)
1 more