6ILX

Crystal structure of PETase W159F mutant from Ideonella sakaiensis

6ILX の概要

• エントリーDOI: 10.2210/pdb6ilx/pdb
• 分子名称: Poly(ethylene terephthalate) hydrolase, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: mutation, hydrolase
• 由来する生物種: Ideonella sakaiensis (strain 201-F6)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28560.05

構造登録者

Liu, C.C.,Shi, C. (登録日: 2018-10-20, 公開日: 2019-03-27, 最終更新日: 2024-11-06)

主引用文献

Liu, C.,Shi, C.,Zhu, S.,Wei, R.,Yin, C.C.
Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.
Biochem. Biophys. Res. Commun., 508:289-294, 2019

PubMed Abstract: Polyethylene terephthalate (PET) hydrolase from Ideonella sakaiensis (IsPETase) can be used to degrade PET. In order to use IsPETase in industry, we studied the enzymatic activity of IsPETase in different conditions containing environmental and physicochemical factors commonly found in nature. We observed that salts and glycerol enhanced the enzymatic activity, while detergents and organic solvents reduced the enzymatic activity. IsPETase hydrolyzed p-nitrophenyl (p-NP) esters instead of naphthyl esters. To make IsPETase an enzyme capable of hydrolyzing naphthyl esters, site-directed mutagenesis was carried out based on the structural information provided by the crystal structure. We found that the IsPETase, IsPETase, and IsPETase mutants can hydrolyze naphthyl esters. IsPETase engineering can direct researchers to use this α/β-hydrolase protein scaffold to design enzymes that can hydrolyze a variety of polyesters.

PubMed: 30502092
DOI: 10.1016/j.bbrc.2018.11.148

実験手法

X-RAY DIFFRACTION (1.45 Å)