› 1x0l

X-ray diffraction
1.85Å resolution

Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus

Released:
DOI: 10.2210/pdb1x0l/pdb
PDB entry 1x0l coloured by chain, front view.
PDB entry 1x0l coloured by chain, side view.
PDB entry 1x0l coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance.
Miyazaki J, Asada K, Fushinobu S, Kuzuyama T, Nishiyama M
J Bacteriol 187 6779-88 (2005)
PMID: 16166541

Function and Biology Details

Reaction catalysed: 
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD(+) = 2-oxoadipate + CO(2) + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180847 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate/homoisocitrate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 333 amino acids
Theoretical weight: 35.84 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72IW9 (Residues: 2-334; Coverage: 100%)
Gene names: TT_C1012, hdh, hicd, hicdh
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2221
Unit cell:
a: 60.963Å b: 143.243Å c: 177.846Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.248
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Convergent strategies in biosynthesis.
Dairi et al. (2011)
1 more

4 mentions without citation

Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance.
Miyazaki et al. (2005)
3 more