4CG2

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

Summary for 4CG2

• Entry DOI: 10.2210/pdb4cg2/pdb
• Related: 4CG1 4CG3
• Descriptor: CUTINASE, phenylmethanesulfonic acid, SULFATE ION, ... (4 entities in total)
• Functional Keywords: pet degradation, hydrolase, alpha beta fold
• Biological source: THERMOBIFIDA FUSCA
• Total number of polymer chains: 1
• Total formula weight: 31191.65

Authors

Roth, C.,Wei, R.,Oeser, T.,Then, J.,Foellner, C.,Zimmermann, W.,Straeter, N. (deposition date: 2013-11-20, release date: 2014-06-25, Last modification date: 2024-11-06)

Primary citation

Roth, C.,Wei, R.,Oeser, T.,Then, J.,Follner, C.,Zimmermann, W.,Strater, N.
Structural and Functional Studies on a Thermostable Polyethylene Terephthalate Degrading Hydrolase from Thermobifida Fusca.
Appl.Microbiol.Biotechnol., 98:7815-, 2014

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.

PubMed: 24728714
DOI: 10.1007/S00253-014-5672-0

Experimental method

X-RAY DIFFRACTION (1.437 Å)