2B61

Crystal Structure of Homoserine Transacetylase

2B61 の概要

• エントリーDOI: 10.2210/pdb2b61/pdb
• 分子名称: Homoserine O-acetyltransferase (2 entities in total)
• 機能のキーワード: acyl-enzyme, aspartate pathway, coenzyme a, structure-function studies, alpha-beta hydrolase fold, transferase
• 由来する生物種: Haemophilus influenzae
• 細胞内の位置: Cytoplasm : P45131
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42539.28

構造登録者

Mirza, I.A.,Nazi, I.,Korczynska, M.,Wright, G.D.,Berghuis, A.M. (登録日: 2005-09-29, 公開日: 2005-11-15, 最終更新日: 2024-11-13)

主引用文献

Mirza, I.A.,Nazi, I.,Korczynska, M.,Wright, G.D.,Berghuis, A.M.
Crystal Structure of Homoserine Transacetylase from Haemophilus influenzae Reveals a New Family of alpha/beta-Hydrolases
Biochemistry, 44:15768-15773, 2005

PubMed Abstract: Homoserine transacetylase catalyzes one of the required steps in the biosynthesis of methionine in fungi and several bacteria. We have determined the crystal structure of homoserine transacetylase from Haemophilus influenzae to a resolution of 1.65 A. The structure identifies this enzyme to be a member of the alpha/beta-hydrolase structural superfamily. The active site of the enzyme is located near the end of a deep tunnel formed by the juxtaposition of two domains and incorporates a catalytic triad involving Ser143, His337, and Asp304. A structural basis is given for the observed double displacement kinetic mechanism of homoserine transacetylase. Furthermore, the properties of the tunnel provide a rationale for how homoserine transacetylase catalyzes a transferase reaction vs hydrolysis, despite extensive similarity in active site architecture to hydrolytic enzymes.

PubMed: 16313180
DOI: 10.1021/bi051951y

実験手法

X-RAY DIFFRACTION (1.65 Å)