1PG3

Acetyl CoA Synthetase, Acetylated on Lys609

「1NNN」から置き換えられました

1PG3 の概要

• エントリーDOI: 10.2210/pdb1pg3/pdb
• 関連するPDBエントリー: 1PG4
• 分子名称: acetyl-CoA synthetase, MAGNESIUM ION, COENZYME A, ... (6 entities in total)
• 機能のキーワード: amp-forming; adenylate-forming; thioester-forming; lysine acetylation, ligase
• 由来する生物種: Salmonella enterica
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 147099.53

構造登録者

Gulick, A.M.,Starai, V.J.,Horswill, A.R.,Homick, K.M.,Escalante-Semerena, J.C. (登録日: 2003-05-27, 公開日: 2003-06-03, 最終更新日: 2023-08-16)

主引用文献

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

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: 12627952
DOI: 10.1021/bi0271603

実験手法

X-RAY DIFFRACTION (2.3 Å)