5CT4

Wild-type Bacillus subtilis lipase A with 5% [BMIM][Cl]

5CT4 の概要

• エントリーDOI: 10.2210/pdb5ct4/pdb
• 関連するPDBエントリー: 5CRI 5CT5 5CT6 5CT8 5CT9 5CTA
• 分子名称: Esterase, 1-butyl-3-methyl-1H-imidazol-3-ium, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39225.59

構造登録者

Nordwald, E.M.,Plaks, J.G.,Snell, J.R.,Sousa, M.C.,Kaar, J.L. (登録日: 2015-07-23, 公開日: 2015-11-04, 最終更新日: 2024-03-06)

主引用文献

Nordwald, E.M.,Plaks, J.G.,Snell, J.R.,Sousa, M.C.,Kaar, J.L.
Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure.
Chembiochem, 16:2456-2459, 2015

PubMed Abstract: We present the first crystallographic insight into the interactions of an ionic liquid (IL) with an enzyme, which has widespread implications for stabilizing enzymes in IL media for biocatalysis. Structures of Bacillus subtilis lipase A (lipA) and an IL-stable variant (QM-lipA) were obtained in the presence of increasing concentrations of 1-butyl-3-methylimidazolium chloride ([BMIM][Cl]). These studies revealed that the [BMIM] cation interacts with surface residues through hydrophobic and cation-π interactions. Of specific interest was the disruption of internal stacking interactions of aromatic side chains by [BMIM], which provides structural evidence for the mechanism of enzyme denaturation by ILs. The interaction of [BMIM] and Cl ions with lipA was reduced by the stabilizing mutations Y49E and G158E in QM-lipA. Ultimately, these findings present the molecular basis for stabilizing enzymes from IL-induced inactivation, as well as the selection of ILs that are less denaturing.

PubMed: 26388426
DOI: 10.1002/cbic.201500398

実験手法

X-RAY DIFFRACTION (1.49 Å)