1FWR

CRYSTAL STRUCTURE OF KDPG ALDOLASE DOUBLE MUTANT K133Q/T161K

1FWR の概要

• エントリーDOI: 10.2210/pdb1fwr/pdb
• 関連するPDBエントリー: 1FQ0
• 分子名称: KDPG ALDOLASE, CITRIC ACID (3 entities in total)
• 機能のキーワード: tim barrel, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 67572.30

構造登録者

Naismith, J.H.,Buchanan, L.V. (登録日: 2000-09-24, 公開日: 2000-10-04, 最終更新日: 2024-02-07)

主引用文献

Wymer, N.,Buchanan, L.V.,Henderson, D.,Mehta, N.,Botting, C.H.,Pocivavsek, L.,Fierke, C.A.,Toone, E.J.,Naismith, J.H.
Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli.
Structure, 9:1-10, 2001

PubMed Abstract: Aldolases are carbon bond-forming enzymes that have long been identified as useful tools for the organic chemist. However, their utility is limited in part by their narrow substrate utilization. Site-directed mutagenesis of various enzymes to alter their specificity has been performed for many years, typically without the desired effect. More recently directed evolution has been employed to engineer new activities onto existing scaffoldings. This approach allows random mutation of the gene and then selects for fitness to purpose those proteins with the desired activity. To date such approaches have furnished novel activities through multiple mutations of residues involved in recognition; in no instance has a key catalytic residue been altered while activity is retained.

PubMed: 11342129
DOI: 10.1016/S0969-2126(00)00555-4

実験手法

X-RAY DIFFRACTION (2.7 Å)