7C4D

Marine microorganism esterase

7C4D の概要

• エントリーDOI: 10.2210/pdb7c4d/pdb
• 分子名称: Putative esterase, 1,2-ETHANEDIOL, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30925.47

構造登録者

Zhu, C.H.,Wu, Y.K.,Isupov, M.N. (登録日: 2020-05-16, 公開日: 2021-05-26, 最終更新日: 2023-11-29)

主引用文献

Zhu, C.,Chen, Y.,Isupov, M.N.,Littlechild, J.A.,Sun, L.,Liu, X.,Wang, Q.,Gong, H.,Dong, P.,Zhang, N.,Wu, Y.
Structural Insights into a Novel Esterase from the East Pacific Rise and Its Improved Thermostability by a Semirational Design.
J.Agric.Food Chem., 69:1079-1090, 2021

PubMed Abstract: Lipolytic enzymes are essential biocatalysts in food processing as well as pharmaceutical and pesticide industries, catalyzing the cleavage of ester bonds in a variety of acyl chain substrates. Here, we report the crystal structure of an esterase from the deep-sea hydrothermal vent of the East Pacific Rise (EprEst). The X-ray structure of EprEst in complex with the ligand, acetate, has been determined at 2.03 Å resolution. The structure reveals a unique spatial arrangement and orientation of the helix cap domain and α/β hydrolase domain, which form a substrate pocket with preference for short-chain acyl groups. Molecular docking analysis further demonstrated that the active site pocket could accommodate -nitrophenyl (NP) carboxyl ligands of varying lengths (≤6 C atoms), with NP-butyrate ester predicted to have the highest binding affinity. Additionally, the semirational design was conducted to improve the thermostability of EprEst by enzyme engineering based on the established structure and multiple sequence alignment. A mutation, K114P, introduced in the hinge region of the esterase, which displayed increased thermostability and enzyme activity. Collectively, the structural and functional data obtained herein could be used as basis for further protein engineering to ultimately expand the scope of industrial applications of marine-derived lipolytic enzymes.

PubMed: 33445864
DOI: 10.1021/acs.jafc.0c06338

実験手法

X-RAY DIFFRACTION (2.03 Å)