› 1dqu

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS

Released:
DOI: 10.2210/pdb1dqu/pdb
PDB entry 1dqu coloured by chain, front view.
PDB entry 1dqu coloured by chain, side view.
PDB entry 1dqu coloured by chain, top view.
Source organism: Aspergillus nidulans
Primary publication:
The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans.
Britton K, Langridge S, Baker PJ, Weeradechapon K, Sedelnikova SE, De Lucas JR, Rice DW, Turner G
Structure 8 349-62 (2000)
PMID: 10801489

Function and Biology Details

Reactions catalysed: 
Isocitrate = succinate + glyoxylate
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151191 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate lyase Chain: A
Molecule details ›
Chain: A
Length: 538 amino acids
Theoretical weight: 60.4 KDa
Source organism: Aspergillus nidulans
Expression system: Aspergillus nidulans
UniProt:
  • Canonical: P28298 (Residues: 1-16, 18-538; Coverage: 100%)
Gene names: AN5634, acuD
Sequence domains: Isocitrate lyase family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P42212
Unit cell:
a: 91.93Å b: 91.93Å c: 152.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.276 0.273 0.376
Expression system: Aspergillus nidulans

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Citations

4 review citations

Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis.
Dunn et al. (2009)
3 more

7 mentions without citation

Potential inhibitors for isocitrate lyase of Mycobacterium tuberculosis and non-M. tuberculosis: a summary.
Lee et al. (2015)
6 more