Structure Report for: 4CG3

Roth, C., Wei, R., Oeser, T., Then, J., Foellner, C., Zimmermann, W., Straeter, N.

Title: 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
Ref: Applied Microbiology & Biotechnology, 98:7815, 2014 : PubMed
Abstract


ESTHER: Roth_2014_Appl.Microbiol.Biotechnol_98_7815
PubMedSearch: Roth 2014 Appl.Microbiol.Biotechnol 98 7815
PubMedID: 24728714
Gene_locus related to this paper: thefu-q6a0i4

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.