page_title: Acetyl-CoA synthetase
section_title: Structure
hierarchical_section_title: Acetyl-CoA synthetase / Structure
caption_attribution_description: English: Ligands bound to active site of ACS
context_page_description: Acetyl-CoA synthetase or Acetate-CoA ligase is an enzyme involved in metabolism of acetate. It is in the ligase class of enzymes, meaning that it catalyzes the formation of a new chemical bond between two large molecules.
context_section_description: The three dimensional structure of the asymmetric ACS (RCSB PDB ID number: 1PG3) reveals that it is composed of two subunits. Each subunit is then composed primarily of two domains. The larger N-terminal domain is composed of 517 residues, while the smaller C-terminal domain is composed of 130 residues. Each subunit has an active site where the ligands are held. The crystallized structure of ACS was determined with CoA and Adenosine- 5′-propylphosphate bound to the enzyme. The reason for using Adenosine- 5′-propylphosphate is that it is an ATP competitive inhibitor which prevents any conformational changes to the enzyme. The adenine ring of AMP/ATP is held in a hydrophobic pocket create by residues Ile (512) and Trp (413).
  The source for the crystallized structure is the organism  Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). The gene for ACS was then transfected into Escherichia coli BL21(DE3) for expression. During chromatography in the process to isolate the enzyme, the subunits came out individually and the total structure was determined separately. The method used to determine the structure was X-ray diffraction with a resolution of 2.3 angstroms. The unit cell values and angles are provided in the following table:
caption: Axial view of ACS (1PG3) showing ligands bound to active site.  Ligands used for crystallization (in image) are adenosine-5'-propylphosphate, CoA and ethanediol.
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