Summary for 1PG4
| Entry DOI | 10.2210/pdb1pg4/pdb |
| Related | 1PG3 |
| Descriptor | acetyl-CoA synthetase, CHLORIDE ION, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | amp-forming; adenylate-forming; thioester-forming, ligase |
| Biological source | Salmonella enterica |
| Total number of polymer chains | 2 |
| Total formula weight | 147108.37 |
| Authors | Gulick, A.M.,Starai, V.J.,Horswill, A.R.,Homick, K.M.,Escalante-Semerena, J.C. (deposition date: 2003-05-27, release date: 2003-06-03, Last modification date: 2024-02-14) |
| Primary citation | Gulick, A.M.,Starai, V.J.,Horswill, A.R.,Homick, K.M.,Escalante-Semerena, J.C. The 1.75 A Crystal Structure of Acetyl-CoA Synthetase Bound to Adenosine-5'-propylphosphate and Coenzyme A Biochemistry, 42:2866-2873, 2003 Cited by PubMed Abstract: 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. PubMed: 12627952DOI: 10.1021/bi0271603 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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