1pg3
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Acetyl CoA Synthetase, Acetylated on Lys609
OverviewOverview
Acetyl-coenzyme A synthetase catalyzes the two-step synthesis of, acetyl-CoA from acetate, ATP, and CoA and belongs to a family of, adenylate-forming enzymes that generate an acyl-AMP intermediate. This, family includes other acyl- and aryl-CoA synthetases, firefly luciferase, and the adenylation domains of the modular nonribosomal peptide, synthetases. We have determined the X-ray crystal structure of acetyl-CoA, synthetase complexed with adenosine-5'-propylphosphate and CoA. The, structure identifies the CoA binding pocket as well as a new conformation, for members of this enzyme family in which the approximately 110-residue, C-terminal domain exhibits a large rotation compared to structures of, peptide synthetase adenylation domains. This domain movement presents a, new set of residues to the active site and removes a conserved lysine, residue that was previously shown to be important for catalysis of the, adenylation half-reaction. Comparison of our structure with kinetic and, structural data of closely related enzymes suggests that the members of, the adenylate-forming family of enzymes may adopt two different, orientations to catalyze the two half-reactions. Additionally, we provide, a structural explanation for the recently shown control of enzyme activity, by acetylation of an active site lysine.
About this StructureAbout this Structure
1PG3 is a Single protein structure of sequence from Salmonella enterica with MG, COA, PRX and EDO as ligands. This structure superseeds the now removed PDB entry 1NNN. Active as Acetate--CoA ligase, with EC number 6.2.1.1 Full crystallographic information is available from OCA.
ReferenceReference
The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A., Gulick AM, Starai VJ, Horswill AR, Homick KM, Escalante-Semerena JC, Biochemistry. 2003 Mar 18;42(10):2866-73. PMID:12627952
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