› 4eu6

X-ray diffraction
1.99Å resolution

Succinyl-CoA:acetate CoA-transferase (AarCH6) in complex with CoA, acetate, and covalent acetylglutamyl anhydride and glutamyl-CoA thioester adducts

Released:
DOI: 10.2210/pdb4eu6/pdb
PDB entry 4eu6 coloured by chain, front view.
PDB entry 4eu6 coloured by chain, side view.
PDB entry 4eu6 coloured by chain, top view.
Source organism: Acetobacter aceti
Primary publication:
Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate CoA-transferase reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases.
Mullins EA, Kappock TJ
Biochemistry 51 8422-34 (2012)
PMID: 23030530

Function and Biology Details

Reaction catalysed: 
Succinyl-CoA + acetate = acetyl-CoA + succinate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-502622 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Succinyl-CoA:acetate CoA-transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 514 amino acids
Theoretical weight: 56.05 KDa
Source organism: Acetobacter aceti
Expression system: Escherichia coli
UniProt:
  • Canonical: B3EY95 (Residues: 1-505; Coverage: 100%)
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand COA 2 x COA
Ligand CL 4 x CL
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 67.168Å b: 110.414Å c: 119.823Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.164 0.208
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Specificity in transition state binding: the Pauling model revisited.
Amyes et al. (2013)
1 more

3 mentions without citation

Structural snapshots along the reaction pathway of Yersinia pestis RipA, a putative butyryl-CoA transferase.
Torres et al. (2014)
2 more