4CG1

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

4CG1 の概要

• エントリーDOI: 10.2210/pdb4cg1/pdb
• 関連するPDBエントリー: 4CG2 4CG3
• 分子名称: CUTINASE, SULFATE ION (3 entities in total)
• 機能のキーワード: pet degradation, hydrolase, alpha beta fold
• 由来する生物種: THERMOBIFIDA FUSCA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30827.32

構造登録者

Roth, C.,Wei, R.,Oeser, T.,Then, J.,Foellner, C.,Zimmermann, W.,Straeter, N. (登録日: 2013-11-20, 公開日: 2014-06-25, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.4 Å)