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Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca
Authors:Christian Roth  Ren Wei  Thorsten Oeser  Johannes Then  Christina Föllner  Wolfgang Zimmermann  Norbert Sträter
Institution:1. Institut für Bioanalytische Chemie, Fakult?t für Chemie und Mineralogie, Universit?t Leipzig, Leipzig, Germany
3. York Structural Biology Laboratory, Department of Chemistry, The University of York, York, YO10 5DD, UK
2. Institut für Biochemie, Fakult?t für Biowissenschaften, Pharmazie und Psychologie, Universit?t Leipzig, Leipzig, Germany
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.
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