4cg3 | pdb_00004cg3

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

spinqualitylabelsall models 4cg3, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cg3 is a 1 chain structure with sequence from "thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 4cg1, 4cg2 Activity: Cutinase, with EC number 3.1.1.74 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMed 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. 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 Appl Microbiol Biotechnol. 2014 Apr 13. PMID:24728714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cutinase

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