9I50

Crystal structure of feruloyl esterase from Fusarium oxysporum G122S variant

Summary for 9I50

• Entry DOI: 10.2210/pdb9i50/pdb
• Related: 6FAT 8BHH
• Descriptor: Carboxylic ester hydrolase, CALCIUM ION, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• Functional Keywords: plastic degrading enzyme, hydrolase
• Biological source: Fusarium oxysporum
• Total number of polymer chains: 2
• Total formula weight: 133552.28

Authors

Karampa, P.,Dimarogona, M.,Topakas, E.,Makryniotis, K.,Nikolaivits, E. (deposition date: 2025-01-27, release date: 2026-04-01)

Primary citation

Karampa, P.,Makryniotis, K.,Sousani, T.I.,Topakas, E.,Daskalakis, V.,Dimarogona, M.
Structural insights into an engineered feruloyl esterase with improved MHET degrading properties.
Febs Lett., 2026

PubMed Abstract: 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.

PubMed: 41797379
DOI: 10.1002/1873-3468.70322

Experimental method

X-RAY DIFFRACTION (1.9 Å)