› 1a59

X-ray diffraction
2.09Å resolution

COLD-ACTIVE CITRATE SYNTHASE

Released:
DOI: 10.2210/pdb1a59/pdb
PDB entry 1a59 coloured by chain, front view.
PDB entry 1a59 coloured by chain, side view.
PDB entry 1a59 coloured by chain, top view.
Source organism: Antarctic bacterium DS2-3R
Primary publication:
Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium.
Russell RJ, Gerike U, Danson MJ, Hough DW, Taylor GL
Structure 6 351-61 (1998)
PMID: 9551556

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Propanoyl-CoA + H(2)O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128515 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-methylcitrate synthase Chain: A
Molecule details ›
Chain: A
Length: 378 amino acids
Theoretical weight: 41.75 KDa
Source organism: Antarctic bacterium DS2-3R
Expression system: Escherichia coli
UniProt:
  • Canonical: O34002 (Residues: 2-379; Coverage: 100%)
Gene names: cisY, gltA
Sequence domains: Citrate synthase, C-terminal domain
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 1 x COA
1 bound ligand:
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P6522
Unit cell:
a: 70.8Å b: 70.8Å c: 307.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.236
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Psychrophilic enzymes: hot topics in cold adaptation.
Feller et al. (2003)
24 more

4 mentions without citation

Psychrophilic enzymes: from folding to function and biotechnology.
Feller G. (2013)
3 more