1pg4
From Proteopedia
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , and | ||||||
| Gene: | ACS (Salmonella enterica) | ||||||
| Activity: | Acetate--CoA ligase, with EC number 6.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Acetyl CoA Synthetase, Salmonella enterica
Overview
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 Structure
1PG4 is a Single protein structure of sequence from Salmonella enterica. This structure supersedes the now removed PDB entry 1NNM. Full crystallographic information is available from OCA.
Reference
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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