7VMD

Crystal structure of a hydrolases Ple628 from marine microbial consortium

7VMD の概要

• エントリーDOI: 10.2210/pdb7vmd/pdb
• 分子名称: hydrolase Ple628, CALCIUM ION (3 entities in total)
• 機能のキーワード: degradation, hydrolase
• 由来する生物種: unclassified Marinobacter
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31308.28

構造登録者

Wu, P.,Zhao, Y.P.,Li, Z.S.,Ingrid, M.C.,Lara, P.,Gao, J.,Han, X.,Li, Q.,Basak, O.,Liu, W.D.,Wei, R. (登録日: 2021-10-08, 公開日: 2022-08-24, 最終更新日: 2024-11-06)

主引用文献

Meyer Cifuentes, I.E.,Wu, P.,Zhao, Y.,Liu, W.,Neumann-Schaal, M.,Pfaff, L.,Barys, J.,Li, Z.,Gao, J.,Han, X.,Bornscheuer, U.T.,Wei, R.,Ozturk, B.
Molecular and Biochemical Differences of the Tandem and Cold-Adapted PET Hydrolases Ple628 and Ple629, Isolated From a Marine Microbial Consortium.
Front Bioeng Biotechnol, 10:930140-930140, 2022

PubMed Abstract: Polybutylene adipate terephthalate (PBAT) is a biodegradable alternative to polyethylene and can be broadly used in various applications. These polymers can be degraded by hydrolases of terrestrial and aquatic origin. In a previous study, we identified tandem PETase-like hydrolases (Ples) from the marine microbial consortium I1 that were highly expressed when a PBAT blend was supplied as the only carbon source. In this study, the tandem Ples, Ple628 and Ple629, were recombinantly expressed and characterized. Both enzymes are mesophilic and active on a wide range of oligomers. The activities of the Ples differed greatly when model substrates, PBAT-modified polymers or PET nanoparticles were supplied. Ple629 was always more active than Ple628. Crystal structures of Ple628 and Ple629 revealed a structural similarity to other PETases and can be classified as member of the PETases IIa subclass, α/β hydrolase superfamily. Our results show that the predicted functions of Ple628 and Ple629 agree with the bioinformatic predictions, and these enzymes play a significant role in the plastic degradation by the consortium.

PubMed: 35935485
DOI: 10.3389/fbioe.2022.930140

実験手法

X-RAY DIFFRACTION (1.69 Å)