› 1zor

X-ray diffraction
2.24Å resolution

Isocitrate dehydrogenase from the hyperthermophile Thermotoga maritima

Released:
DOI: 10.2210/pdb1zor/pdb
PDB entry 1zor coloured by chain, front view.
PDB entry 1zor coloured by chain, side view.
PDB entry 1zor coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
The crystal structure of a hyperthermostable subfamily II isocitrate dehydrogenase from Thermotoga maritima.
Karlström M, Steen IH, Madern D, Fedöy AE, Birkeland NK, Ladenstein R
FEBS J 273 2851-68 (2006)
PMID: 16759231

Function and Biology Details

Reaction catalysed: 
(1a) isocitrate + NADP(+) = 2-oxalosuccinate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194729 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase [NADP] Chains: A, B
Molecule details ›
Chains: A, B
Length: 399 amino acids
Theoretical weight: 45.47 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0N2 (Residues: 1-399; Coverage: 100%)
Gene name: TM_1148
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

1 bound ligand:
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 62.47Å b: 88.051Å c: 180.926Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.223
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Nature versus nurture: developing enzymes that function under extreme conditions.
Liszka et al. (2012)
17 other articles

3 mentions without citation

Functional relevance of dynamic properties of Dimeric NADP-dependent Isocitrate Dehydrogenases.
Vinekar et al. (2012)
2 more