6SCD

Polyester hydrolase PE-H Y250S mutant of Pseudomonas aestusnigri

6SCD の概要

• エントリーDOI: 10.2210/pdb6scd/pdb
• 関連するPDBエントリー: 6SBN
• 分子名称: Polyester hydrolase, SULFATE ION, PHOSPHATE ION, ... (9 entities in total)
• 機能のキーワード: polyester degradation, pet hydrolase, marine bacteria, pseudomonas aestusnigri, hydrolase
• 由来する生物種: Pseudomonas aestusnigri
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67563.75

構造登録者

Bollinger, A.,Thies, S.,Kobus, S.,Hoeppner, A.,Smits, S.H.J.,Jaeger, K.-E. (登録日: 2019-07-24, 公開日: 2020-02-26, 最終更新日: 2024-11-20)

主引用文献

Bollinger, A.,Thies, S.,Knieps-Grunhagen, E.,Gertzen, C.,Kobus, S.,Hoppner, A.,Ferrer, M.,Gohlke, H.,Smits, S.H.J.,Jaeger, K.E.
A Novel Polyester Hydrolase From the Marine BacteriumPseudomonas aestusnigri -Structural and Functional Insights.
Front Microbiol, 11:114-114, 2020

PubMed Abstract: Biodegradation of synthetic polymers, in particular polyethylene terephthalate (PET), is of great importance, since environmental pollution with PET and other plastics has become a severe global problem. Here, we report on the polyester degrading ability of a novel carboxylic ester hydrolase identified in the genome of the marine hydrocarbonoclastic bacterium VGXO14 . The enzyme, designated PE-H, belongs to the type IIa family of PET hydrolytic enzymes as indicated by amino acid sequence homology. It was produced in , purified and its crystal structure was solved at 1.09 Å resolution representing the first structure of a type IIa PET hydrolytic enzyme. The structure shows a typical α/β-hydrolase fold and high structural homology to known polyester hydrolases. PET hydrolysis was detected at 30°C with amorphous PET film (PETa), but not with PET film from a commercial PET bottle (PETb). A rational mutagenesis study to improve the PET degrading potential of PE-H yielded variant PE-H (Y250S) which showed improved activity, ultimately also allowing the hydrolysis of PETb. The crystal structure of this variant solved at 1.35 Å resolution allowed to rationalize the improvement of enzymatic activity. A PET oligomer binding model was proposed by molecular docking computations. Our results indicate a significant potential of the marine bacterium for PET degradation.

PubMed: 32117139
DOI: 10.3389/fmicb.2020.00114

実験手法

X-RAY DIFFRACTION (1.35 Å)