4CG2

Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.44 Å
  • R-Value Free: 0.166 
  • R-Value Work: 0.138 
  • R-Value Observed: 0.141 

Starting Model: experimental
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Literature

Structural and Functional Studies on a Thermostable Polyethylene Terephthalate Degrading Hydrolase from Thermobifida Fusca.

Roth, C., Wei, R., Oeser, T., Then, J., Follner, C., Zimmermann, W., Strater, N.

(2014) Appl Microbiol Biotechnol 98: 7815

  • DOI: https://doi.org/10.1007/s00253-014-5672-0
  • Primary Citation of Related Structures:  
    4CG1, 4CG2, 4CG3

  • PubMed Abstract: 

    Bacterial cutinases are promising catalysts for the modification and degradation of the widely used plastic polyethylene terephthalate (PET). The improvement of the enzyme for industrial purposes is limited due to the lack of structural information for cutinases of bacterial origin. We have crystallized and structurally characterized a cutinase from Thermobifida fusca KW3 (TfCut2) in free as well as in inhibitor-bound form. Together with our analysis of the thermal stability and modelling studies, we suggest possible reasons for the outstanding thermostability in comparison to the less thermostable homolog from Thermobifida alba AHK119 and propose a model for the binding of the enzyme towards its polymeric substrate. The TfCut2 structure is the basis for the rational design of catalytically more efficient enzyme variants for the hydrolysis of PET and other synthetic polyesters.

    • Organizational Affiliation: 

    Institut für Bioanalytische Chemie, Fakultät für Chemie und Mineralogie, Universität Leipzig, Leipzig, Germany, [email protected].


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CUTINASE282Thermobifida fuscaMutation(s): 0 
EC: 3.1.1.74 (PDB Primary Data), 3.1.1.101 (UniProt)
UniProt
Find proteins for Q6A0I4 (Thermobifida fusca)
Explore Q6A0I4 
Go to UniProtKB:  Q6A0I4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6A0I4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.44 Å
  • R-Value Free: 0.166 
  • R-Value Work: 0.138 
  • R-Value Observed: 0.141 
  • Space Group: I 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 116.591α = 90
b = 116.591β = 90
c = 35.581γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-06-25
    Type: Initial release
  • Version 1.1: 2014-09-10
    Changes: Database references
  • Version 2.0: 2019-10-23
    Changes: Atomic model, Data collection, Derived calculations, Other
  • Version 2.1: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 2.2: 2024-11-06
    Changes: Structure summary