3O4F

Crystal Structure of Spermidine Synthase from E. coli

「3ADN」から置き換えられました 「3HH9」から置き換えられました

3O4F の概要

• エントリーDOI: 10.2210/pdb3o4f/pdb
• 分子名称: Spermidine synthase, SULFATE ION (3 entities in total)
• 機能のキーワード: aminopropyltransferase, polyamine synthase, rossmann fold, polyamine biosynthesis, spermidine biosynthesis, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 268459.67

構造登録者

Zhou, X.,Tkaczuk, K.L.,Chruszcz, M.,Chua, T.K.,Minor, W.,Sivaraman, J. (登録日: 2010-07-27, 公開日: 2010-08-18, 最終更新日: 2023-11-01)

主引用文献

Zhou, X.,Chua, T.K.,Tkaczuk, K.L.,Bujnicki, J.M.,Sivaraman, J.
The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket
J.Struct.Biol., 169:277-285, 2010

PubMed Abstract: Polyamines are essential in all branches of life. Biosynthesis of spermidine, one of the most ubiquitous polyamines, is catalyzed by spermidine synthase (SpeE). Although the function of this enzyme from Escherichia coli has been thoroughly characterised, its structural details remain unknown. Here, we report the crystal structure of E. coli SpeE and study its interaction with the ligands by isothermal titration calorimetry and computational modelling. SpeE consists of two domains - a small N-terminal beta-strand domain, and a C-terminal catalytic domain that adopts a canonical methyltransferase (MTase) Rossmann fold. The protein forms a dimer in the crystal and in solution. Structural comparison of E. coli SpeE to its homologs reveals that it has a large and unique substrate-binding cleft that may account for its lower amine substrate specificity.

PubMed: 20051267
DOI: 10.1016/j.jsb.2009.12.024

実験手法

X-RAY DIFFRACTION (2.9 Å)