› 4jag

X-ray diffraction
2.1Å resolution

STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE FROM E. COLI COMPLEXED WITH oxaloacetate

Released:
DOI: 10.2210/pdb4jag/pdb
PDB entry 4jag coloured by chain, front view.
PDB entry 4jag coloured by chain, side view.
PDB entry 4jag coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Enzyme-substrate complexes of allosteric citrate synthase: evidence for a novel intermediate in substrate binding.
Duckworth HW, Nguyen NT, Gao Y, Donald LJ, Maurus R, Ayed A, Bruneau B, Brayer GD
Biochim Biophys Acta 1834 2546-53 (2013)
PMID: 23954305

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142164 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Citrate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 426 amino acids
Theoretical weight: 47.99 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABH7 (Residues: 2-427; Coverage: 100%)
Gene names: JW0710, b0720, gltA, gluT, icdB
Sequence domains: Citrate synthase, C-terminal domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand OAA 2 x OAA
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: R3
Unit cell:
a: 165.152Å b: 165.152Å c: 158.841Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.182 0.21
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion.
Nguyen et al. (2019)
2 more

1 mention without citation

Proteomic Profiling, Transcription Factor Modeling, and Genomics of Evolved Tolerant Strains Elucidate Mechanisms of Vanillin Toxicity in Escherichia coli.
Pattrick et al. (2019)