› 1owc

X-ray diffraction
2.2Å resolution

Three Dimensional Structure Analysis Of The R109L Variant of the Type II Citrate Synthase From E. Coli

Released:
DOI: 10.2210/pdb1owc/pdb
PDB 1owc coloured by chain and viewed from the front.
PDB 1owc coloured by chain and viewed from the side.
PDB 1owc coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
Probing the roles of key residues in the unique regulatory NADH binding site of type II citrate synthase of Escherichia coli.
Stokell DJ, Donald LJ, Maurus R, Nguyen NT, Sadler G, Choudhary K, Hultin PG, Brayer GD, Duckworth HW
J. Biol. Chem. 278 35435-43 (2003)
PMID: 12824188

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Citrate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 427 amino acids
Theoretical weight: 48.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABH7 (Residues: 1-427; Coverage: 100%)
Gene names: JW0710, b0720, gltA, gluT, icdB
Sequence domains: Citrate synthase, C-terminal domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: R3
Unit cell:
a: 165.07Å b: 165.07Å c: 155.293Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.161 0.21
Expression system: Escherichia coli

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Citations

1 review citation

Optimization of enzyme parameters for fermentative production of biorenewable fuels and chemicals.
Jarboe et al. (2012)
16 other articles