› 2ahw

X-ray diffraction
2.15Å resolution

Crystal Structure of Acyl-CoA transferase from E. coli O157:H7 (YdiF)-thioester complex with CoA- 2

Released:
DOI: 10.2210/pdb2ahw/pdb
PDB entry 2ahw coloured by chain, front view.
PDB entry 2ahw coloured by chain, side view.
PDB entry 2ahw coloured by chain, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases.
Rangarajan ES, Li Y, Ajamian E, Iannuzzi P, Kernaghan SD, Fraser ME, Cygler M, Matte A
J Biol Chem 280 42919-28 (2005)
PMID: 16253988

Function and Biology Details

Reaction catalysed: 
Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186842 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetate CoA-transferase YdiF Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 531 amino acids
Theoretical weight: 57.57 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8X5X6 (Residues: 1-531; Coverage: 100%)
Gene names: ECs2401, Z2722, ydiF
Sequence domains: Coenzyme A transferase
Structure domains: Glutaconate Coenzyme A-transferase

Ligands and Environments

1 bound ligand:
Ligand COA 3 x COA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 80.883Å b: 137.095Å c: 110.424Å
α: 90° β: 105.83° γ: 90°
R-values:
R R work R free
0.191 0.186 0.235
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Acetate formation in the energy metabolism of parasitic helminths and protists.
Tielens et al. (2010)
18 other articles