9i50 | pdb_00009i50

Crystal structure of feruloyl esterase from Fusarium oxysporum G122S variant

spinqualitylabelsall models 9i50, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9i50 is a 2 chain structure with sequence from Fusarium oxysporum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: BMA, CA, EDO, MAN, NAG, PEG, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1D3S5H0_FUSOX Publication Abstract from PubMed Mono(2-hydroxyethyl) terephthalate (MHET) esterases (MHETases) are enzymes implicated in polyethylene terephthalate (PET) biodegradation. The present study elucidates the structural determinants that result in increased MHET degradation by a feruloyl esterase, which has been engineered to resemble the MHETase active site. The crystal structures of the variant in apo- and benzoic acid bound states reveal the changes induced by the introduced mutation, specifically the formation of a hydrogen bond and a trans to cis isomerization of a peptide bond in the vicinity of the catalytic site. Molecular dynamics simulations demonstrate the stabilization of the loop harboring the engineered residue, as well as an expansion of the substrate binding cleft, which would facilitate accommodation of a broader variety of substrates, indicative of a promiscuous biocatalyst. Structural insights into an engineered feruloyl esterase with improved MHET degrading properties.,Karampa P, Makryniotis K, Sousani TI, Topakas E, Daskalakis V, Dimarogona M FEBS Lett. 2026 Mar 8. doi: 10.1002/1873-3468.70322. PMID:41797379 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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