› 1gc5

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS

Released:
DOI: 10.2210/pdb1gc5/pdb
PDB entry 1gc5 coloured by chain, front view.
PDB entry 1gc5 coloured by chain, side view.
PDB entry 1gc5 coloured by chain, top view.
Source organism: Thermococcus litoralis
Primary publication:
Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon.
Ito S, Fushinobu S, Yoshioka I, Koga S, Matsuzawa H, Wakagi T
Structure 9 205-14 (2001)
PMID: 11286887

Function and Biology Details

Reaction catalysed: 
ADP + D-glucosamine = AMP + D-glucosamine 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181705 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-dependent glucose/glucosamine kinase Chain: A
Molecule details ›
Chain: A
Length: 467 amino acids
Theoretical weight: 53.62 KDa
Source organism: Thermococcus litoralis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7M537 (Residues: 1-467; Coverage: 100%)
Gene names: OCC_09701, glkA
Sequence domains: ADP-specific Phosphofructokinase/Glucokinase conserved region
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P3221
Unit cell:
a: 109.8Å b: 109.8Å c: 129.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 0.252
Expression system: Escherichia coli

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Citations

8 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
7 more

7 mentions without citation

Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.
Rivas-Pardo et al. (2013)
6 more