2AA9

EPSP synthase liganded with shikimate

2AA9 の概要

• エントリーDOI: 10.2210/pdb2aa9/pdb
• 関連するPDBエントリー: 1G6S 1G6T 1MI4 1Q36 1X8R 1X8T
• 分子名称: 3-phosphoshikimate 1-carboxyvinyltransferase, (3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: inside-out alpha/beta barrel, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P0A6D3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47098.19

構造登録者

Priestman, M.A.,Healy, M.L.,Funke, T.,Becker, A.,Schonbrunn, E. (登録日: 2005-07-13, 公開日: 2006-02-14, 最終更新日: 2023-08-23)

主引用文献

Priestman, M.A.,Healy, M.L.,Funke, T.,Becker, A.,Schonbrunn, E.
Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate.
Febs Lett., 579:5773-5780, 2005

PubMed Abstract: The shikimate pathway enzyme 5-enolpyruvyl shikimate-3-phosphate synthase (EPSP synthase) has received attention in the past because it is the target of the broad-spectrum herbicide glyphosate. The natural substrate of EPSP synthase is shikimate-3-phosphate. However, this enzyme can also utilize shikimate as substrate. Remarkably, this reaction is insensitive to inhibition by glyphosate. Crystallographic analysis of EPSP synthase from Escherichia coli, in complex with shikimate/glyphosate at 1.5 Angstroms resolution, revealed that binding of shikimate induces changes around the backbone of the active site, which in turn impact the efficient binding of glyphosate. The implications from these findings with respect to the design of novel glyphosate-insensitive EPSP synthase enzymes are discussed.

PubMed: 16225867
DOI: 10.1016/j.febslet.2005.09.066

実験手法

X-RAY DIFFRACTION (1.5 Å)