6ilx | pdb_00006ilx

Crystal structure of PETase W159F mutant from Ideonella sakaiensis

spinqualitylabelsall models 6ilx, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ilx is a 1 chain structure with sequence from Idesa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, NA Gene: ISF6_4831 (IDESA) Activity: Poly(ethylene terephthalate) hydrolase, with EC number 3.1.1.101 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Polyethylene terephthalate (PET) hydrolase from Ideonella sakaiensis (IsPETase) can be used to degrade PET. In order to use IsPETase in industry, we studied the enzymatic activity of IsPETase in different conditions containing environmental and physicochemical factors commonly found in nature. We observed that salts and glycerol enhanced the enzymatic activity, while detergents and organic solvents reduced the enzymatic activity. IsPETase hydrolyzed p-nitrophenyl (p-NP) esters instead of naphthyl esters. To make IsPETase an enzyme capable of hydrolyzing naphthyl esters, site-directed mutagenesis was carried out based on the structural information provided by the crystal structure. We found that the IsPETase(S93M), IsPETase(W159F), and IsPETase(N241F) mutants can hydrolyze naphthyl esters. IsPETase engineering can direct researchers to use this alpha/beta-hydrolase protein scaffold to design enzymes that can hydrolyze a variety of polyesters. Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.,Liu C, Shi C, Zhu S, Wei R, Yin CC Biochem Biophys Res Commun. 2019 Jan 1;508(1):289-294. doi:, 10.1016/j.bbrc.2018.11.148. Epub 2018 Nov 27. PMID:30502092 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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