9Z11
Crystal Structure of the Poly(Hexamethylene Adipamide) (Nylon66) Hydrolase Nyl50 in Complex with Butyrate at Room Temperature
Summary for 9Z11
| Entry DOI | 10.2210/pdb9z11/pdb |
| Descriptor | Poly (Hexamethylene adipamide) hydrolase, butanoic acid (3 entities in total) |
| Functional Keywords | nylon hydrolase, ntn-hydrolase, nylon-66, hydrolase |
| Biological source | Alphaproteobacteria bacterium |
| Total number of polymer chains | 2 |
| Total formula weight | 62998.01 |
| Authors | |
| Primary citation | Capra, N.,Bourgery, C.,Parks, J.M.,Carper, D.L.,Cahill, J.F.,Michener, J.K.,Meilleur, F. Structural and oligomeric characterization of substrate- and product-selective nylon hydrolases. Biorxiv, 2026 Cited by PubMed Abstract: Enzymatic degradation of synthetic polymers has attracted broad interest because it offers environmental and manufacturing advantages compared to traditional mechanical and chemical breakdown approaches. Enzymes are highly specific and reaction conditions are generally aqueous and require low pressure and temperature, resulting in lower energy consumption and lower chemical waste production. Here we report the biochemical and structural characterization of three newly discovered enzymes capable of nylon hydrolysis: Nyl10, Nyl12 and Nyl50. Using solution characterization techniques, we found that the enzymes adopt a single oligomeric state consistent with a tetramer over a wide range of concentrations. X-ray crystallographic structures of all three enzymes support the association into tetramers. Comparison of ligand-bound X-ray crystal structures of Nyl10 and Nyl12 with the previously determined structure of Nyl50 identified key structural determinants involved in ligand binding. Noticeably, a flexible loop found in several polyamide degrading enzymes is observed to flip towards (closed conformation) and away (open conformation) from the active site upon ligand binding. Analysis of adduct and surrogate substrate-bound enzyme complex structures provide a model for substrate binding directionality. Finally, activity assays showed that both Nyl10 and Nyl12 can hydrolyze ester bonds, and that Nyl12 has the highest activity toward PA66, identifying it as the best candidate for protein engineering for efficient nylon hydrolysis. PubMed: 41889879DOI: 10.64898/2026.03.11.711162 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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