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7VMD

Crystal structure of a hydrolases Ple628 from marine microbial consortium

Summary for 7VMD
Entry DOI10.2210/pdb7vmd/pdb
Descriptorhydrolase Ple628, CALCIUM ION (3 entities in total)
Functional Keywordsdegradation, hydrolase
Biological sourceunclassified Marinobacter
Total number of polymer chains1
Total formula weight31308.28
Authors
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. (deposition date: 2021-10-08, release date: 2022-08-24, Last modification date: 2024-11-06)
Primary citationMeyer 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.69 Å)
Structure validation

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数据于2025-07-23公开中

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