8ibi | pdb_00008ibi

Inactive mutant of CtPL-H210S/F214I

spinqualitylabelsall models 8ibi, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ibi is a 2 chain structure with sequence from Caldimonas taiwanensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.14Å Ligands: GOL, NAG, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Using enzymes to hydrolyze and recycle poly(ethylene terephthalate) (PET) is an attractive eco-friendly approach to manage the ever-increasing PET wastes, while one major challenge to realize the commercial application of enzyme-based PET degradation is to establish large-scale production methods to produce PET hydrolytic enzyme. To achieve this goal, we exploited the industrial strain Pichia pastoris to express a PET hydrolytic enzyme from Caldimonas taiwanensis termed CtPL-DM. In contrast to the protein expressed in Escherichia coli, CtPL-DM expressed in P. pastoris is inactive in PET degradation. Structural analysis indicates that a putative N-glycosylation site N181 could restrain the conformational change of a substrate-binding Trp and hamper the enzyme action. We thus constructed N181A to remove the N-glycosylation and found that the PET hydrolytic activity of this variant was restored. The performance of N181A was further enhanced via molecular engineering. These results are of valuable in terms of PET hydrolytic enzyme production in industrial strains in the future. Functional tailoring of a PET hydrolytic enzyme expressed in Pichia pastoris.,Li X, Shi B, Huang JW, Zeng Z, Yang Y, Zhang L, Min J, Chen CC, Guo RT Bioresour Bioprocess. 2023 Apr 6;10(1):26. doi: 10.1186/s40643-023-00648-1. PMID:38647782 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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