title: Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca.
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.
authors.affiliation: Institut für Bioanalytische Chemie, Fakultät für Chemie und Mineralogie, Universität Leipzig, Leipzig, Germany, christian.roth@york.ac.uk.
authors.forename: Christian
authors.initials: C
authors.lastname: Roth
authors.forename: Ren
authors.initials: R
authors.lastname: Wei
authors.forename: Thorsten
authors.initials: T
authors.lastname: Oeser
authors.forename: Johannes
authors.initials: J
authors.lastname: Then
authors.forename: Christina
authors.initials: C
authors.lastname: Föllner
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Zimmermann
authors.forename: Norbert
authors.initials: N
authors.lastname: Sträter
mesh_terms: D000192:Actinomycetales / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D011093:Polyethylene Terephthalates / Q000378:metabolism*
chemical_list: D011093:Polyethylene Terephthalates; D006867:Hydrolases; D002265:Carboxylic Ester Hydrolases; C019952:cutinase