1T3D

Crystal structure of Serine Acetyltransferase from E.coli at 2.2A

1T3D の概要

• エントリーDOI: 10.2210/pdb1t3d/pdb
• 分子名称: Serine acetyltransferase, CYSTEINE (3 entities in total)
• 機能のキーワード: left-handed-beta-helix, dimer of trimers, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A9D4
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 95108.31

構造登録者

Pye, V.E.,Tingey, A.P.,Robson, R.L.,Moody, P.C.E. (登録日: 2004-04-26, 公開日: 2004-07-13, 最終更新日: 2024-10-30)

主引用文献

Pye, V.E.,Tingey, A.P.,Robson, R.L.,Moody, P.C.E.
The Structure and Mechanism of Serine Acetyltransferase from Escherichia coli
J.Biol.Chem., 279:40729-40736, 2004

PubMed Abstract: Serine acetyltransferase (SAT) catalyzes the first step of cysteine synthesis in microorganisms and higher plants. Here we present the 2.2 A crystal structure of SAT from Escherichia coli, which is a dimer of trimers, in complex with cysteine. The SAT monomer consists of an amino-terminal alpha-helical domain and a carboxyl-terminal left-handed beta-helix. We identify His(158) and Asp(143) as essential residues that form a catalytic triad with the substrate for acetyl transfer. This structure shows the mechanism by which cysteine inhibits SAT activity and thus controls its own synthesis. Cysteine is found to bind at the serine substrate site and not the acetyl-CoA site that had been reported previously. On the basis of the geometry around the cysteine binding site, we are able to suggest a mechanism for the O-acetylation of serine by SAT. We also compare the structure of SAT with other left-handed beta-helical structures.

PubMed: 15231846
DOI: 10.1074/jbc.M403751200

実験手法

X-RAY DIFFRACTION (2.2 Å)