› 1ky8

X-ray diffraction
2.4Å resolution

Crystal Structure of the Non-phosphorylating glyceraldehyde-3-phosphate Dehydrogenase

Released:
DOI: 10.2210/pdb1ky8/pdb
PDB entry 1ky8 coloured by chain, front view.
PDB entry 1ky8 coloured by chain, side view.
PDB entry 1ky8 coloured by chain, top view.
Source organism: Thermoproteus tenax
Primary publication:
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.
Pohl E, Brunner N, Wilmanns M, Hensel R
J Biol Chem 277 19938-45 (2002)
PMID: 11842090

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate + NAD(P)(+) + H(2)O = 3-phospho-D-glycerate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129594 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 501 amino acids
Theoretical weight: 54.16 KDa
Source organism: Thermoproteus tenax
Expression system: Escherichia coli
UniProt:
  • Canonical: O57693 (Residues: 1-501; Coverage: 100%)
Gene name: gapN
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B, EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P6222
Unit cell:
a: 185.2Å b: 185.2Å c: 132.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.242
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

N-terminal Gly(224)-Gly(411) domain in Listeria adhesion protein interacts with host receptor Hsp60.
Jagadeesan et al. (2011)