9fz1 | pdb_00009fz1

UMG-SP3 amidase from uncultured bacterium in complex with 4,4'-MDA

spinqualitylabelsall models 9fz1, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9fz1 is a 2 chain structure with sequence from Uncultured bacterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: A1IHK, ACT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Global plastic production exceeded 400 million tons in 2022, urgently demanding improved waste management and recycling strategies for a circular plastic economy. While the enzymatic hydrolysis of polyethylene terephthalate (PET) has become feasible on industrial scales, efficient enzymes targeting other hydrolyzable plastic types, such as polyurethanes (PURs), are lacking. Recently, enzymes of the amidase signature (AS) family, capable of cleaving urethane bonds in a polyether-PUR analog and a linear polyester-PUR, have been identified. Herein, we present high-resolution crystal structures of the AS enzyme UMG-SP3 in three states: ligand-free, bound with a suicidal inhibitor mimicking the transition state, and bound with a monomeric PUR degradation product. Besides revealing the conserved core and catalytic triad akin to other AS family members, the UMG-SP3 structures show remarkable flexibility of loop regions. Particularly, Arg209 in loop 3 adopts two induced-fit conformations upon ligand binding. Through structure-guided kinetic studies and enzyme engineering, we mapped structural key elements that determine the enhanced hydrolysis of urethane and amide bonds in various small molecules, including a linear PUR fragment analog. Our findings contribute critical insights into urethanase activity, aiding PUR degradation campaigns and sustainable plastic recycling efforts in the future. Structural and Functional Characterization of an Amidase Targeting a Polyurethane for Sustainable Recycling.,Rotilio L, Bayer T, Meinert H, Teixeira LMC, Johansen MB, Sommerfeldt A, Petersen AR, Sandahl A, Keller MB, Holck J, Paiva P, Otzen DE, Bornscheuer UT, Wei R, Fernandes PA, Ramos MJ, Westh P, Morth JP Angew Chem Int Ed Engl. 2024 Nov 29:e202419535. doi: 10.1002/anie.202419535. PMID:39611359 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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