7NEI

Polyester Hydrolase Leipzig 7 (PHL7) in the unliganded state


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.30 Å
  • R-Value Free: 0.159 
  • R-Value Work: 0.132 
  • R-Value Observed: 0.133 

Starting Model: in silico
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wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Low Carbon Footprint Recycling of Post-Consumer PET Plastic with a Metagenomic Polyester Hydrolase.

Sonnendecker, C.Oeser, J.Richter, P.K.Hille, P.Zhao, Z.Fischer, C.Lippold, H.Blazquez-Sanchez, P.Engelberger, F.Ramirez-Sarmiento, C.A.Oeser, T.Lihanova, Y.Frank, R.Jahnke, H.G.Billig, S.Abel, B.Strater, N.Matysik, J.Zimmermann, W.

(2022) ChemSusChem 15: e202101062-e202101062

  • DOI: https://doi.org/10.1002/cssc.202101062
  • Primary Citation of Related Structures:  
    7NEI

  • PubMed Abstract: 

    Earth is flooded with plastics and the need for sustainable recycling strategies for polymers has become increasingly urgent. Enzyme-based hydrolysis of post-consumer plastic is an emerging strategy for closed-loop recycling of polyethylene terephthalate (PET). The polyester hydrolase PHL7, isolated from a compost metagenome, completely hydrolyzes amorphous PET films, releasing 91 mg of terephthalic acid per hour and mg of enzyme. Vertical scanning interferometry shows degradation rates of the PET film of 6.8 μm h -1 . Structural analysis indicates the importance of leucine at position 210 for the extraordinarily high PET-hydrolyzing activity of PHL7. Within 24 h, 0.6 mg enzyme  g PET -1 completely degrades post-consumer thermoform PET packaging in an aqueous buffer at 70 °C without any energy-intensive pretreatments. Terephthalic acid recovered from the enzymatic hydrolysate is then used to synthesize virgin PET, demonstrating the potential of polyester hydrolases as catalysts in sustainable PET recycling processes with a low carbon footprint.


  • Organizational Affiliation

    Institute of Analytical Chemistry, Leipzig University, 04103, Leipzig, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Polyester Hydrolase Leipzig 7 (PHL-7)
A, B
267unidentifiedMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.30 Å
  • R-Value Free: 0.159 
  • R-Value Work: 0.132 
  • R-Value Observed: 0.133 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 56.35α = 90
b = 97.68β = 90
c = 101.1γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
MxCuBEdata collection
XDSdata reduction
Aimlessdata scaling
PHASERphasing
Cootmodel building

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2021-06-23
    Type: Initial release
  • Version 1.1: 2022-02-23
    Changes: Database references
  • Version 1.2: 2022-05-18
    Changes: Database references
  • Version 1.3: 2022-11-23
    Changes: Structure summary
  • Version 1.4: 2024-05-01
    Changes: Data collection, Database references, Refinement description
  • Version 1.5: 2024-11-20
    Changes: Structure summary