1RY2

Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP

1RY2 の概要

• エントリーDOI: 10.2210/pdb1ry2/pdb
• 関連するPDBエントリー: 1PG3 1PG4
• 分子名称: acetyl-coenzyme A synthetase 1, ADENOSINE MONOPHOSPHATE (2 entities in total)
• 機能のキーワード: amp forming; related to firefly luciferase, ligase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Microsome : Q01574
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 73950.42

構造登録者

Jogl, G.,Tong, L. (登録日: 2003-12-19, 公開日: 2004-03-09, 最終更新日: 2023-08-23)

主引用文献

Jogl, G.,Tong, L.
Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP
Biochemistry, 43:1425-1431, 2004

PubMed Abstract: Acetyl-coenzyme A synthetase (ACS) belongs to the family of AMP-forming enzymes that also includes acyl-CoA synthetases, firefly luciferase, and nonribosomal peptide synthetases. ACS catalyzes the two-step activation of acetate to acetyl-CoA: formation of an acetyl-AMP intermediate from acetate and ATP and the transfer of the acetyl group to CoA. In mammals, the acetyl-CoA product is used for biosynthesis of long chain fatty acids as well as energy production. We have determined the crystal structure of yeast ACS in a binary complex with AMP at 2.3 A resolution. The structure contains a large, N-terminal domain and a small, C-terminal domain. AMP is bound at the interface between the two domains. This structure represents a new conformation for the ACS enzyme, which may be competent for catalyzing the first step of the reaction. A Lys residue that is critical for this step is located in the active site. A rotation of 140 degrees in the small domain is needed for the binding of CoA and the catalysis of the second step. In contrast to the monomeric bacterial enzyme, yeast ACS is a stable trimer.

PubMed: 14769018
DOI: 10.1021/bi035911a

実験手法

X-RAY DIFFRACTION (2.3 Å)