8S7H

Fructose 6-phosphate aldolase (FSA) from Escherichia coli

8S7H の概要

• エントリーDOI: 10.2210/pdb8s7h/pdb
• EMDBエントリー: 19772
• 分子名称: Fructose-6-phosphate aldolase 1 (1 entity in total)
• 機能のキーワード: fructose 6-phosphate aldolase, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 238956.72

構造登録者

Hebert, H.,Widersten, M. (登録日: 2024-03-01, 公開日: 2025-03-12, 最終更新日: 2025-09-24)

主引用文献

Hebert, H.,Sonmez, E.,Purhonen, P.,Widersten, M.
Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes.
Structure, 32:1322-1326.e4, 2024

PubMed Abstract: Two structures of fructose 6-phosphate aldolase, the wild-type and an engineered variant containing five active-site mutations, have been solved by cryoelectron microscopy (cryo-EM). The engineered variant affords production of aldols from aryl substituted ketones and aldehydes. This structure was solved to a resolution of 3.1 Å and contains the critical iminium reaction intermediate trapped in the active site. This provides new information that rationalizes the acquired substrate scope and aids in formulating hypotheses of the chemical mechanism. A Tyr residue (Y131) is positioned for a role as catalytic acid/base during the aldol reaction and the different structures demonstrate mobility of this amino acid residue. Further engineering of this fructose 6-phosphate aldolase (FSA) variant, guided by this new structure, identified additional FSA variants that display improved carboligation activities with 2-hydroxyacetophenone and phenylacetaldehyde.

PubMed: 39013461
DOI: 10.1016/j.str.2024.06.011

実験手法

ELECTRON MICROSCOPY (2.8 Å)