› 1w96

X-ray diffraction
1.8Å resolution

Crystal Structure of Biotin Carboxylase Domain of Acetyl-coenzyme A Carboxylase from Saccharomyces cerevisiae in Complex with Soraphen A

Released:
DOI: 10.2210/pdb1w96/pdb
PDB entry 1w96 coloured by chain, front view.
PDB entry 1w96 coloured by chain, side view.
PDB entry 1w96 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product.
Shen Y, Volrath SL, Weatherly SC, Elich TD, Tong L
Mol Cell 16 881-91 (2004)
PMID: 15610732

Function and Biology Details

Reactions catalysed: 
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N(6)-L-lysine
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169487 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA carboxylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 554 amino acids
Theoretical weight: 61.65 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00955 (Residues: 13-566; Coverage: 25%)
Gene names: ABP2, ACC1, FAS3, MTR7, N3175, YNR016C
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand S1A 3 x S1A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 63.83Å b: 96.52Å c: 139.95Å
α: 90° β: 96.82° γ: 90°
R-values:
R R work R free
0.195 0.195 0.23
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Fatty acid synthesis and elongation in yeast.
Tehlivets et al. (2007)
23 more

5 mentions without citation

The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.
Waldrop et al. (2012)
4 more