9CXR
X-ray Crystallographic Structure of the Poly(Hexamethylene Adipamide) (Nylon66) Hydrolase Nyl50 at Room Temperature
This is a non-PDB format compatible entry.
Summary for 9CXR
| Entry DOI | 10.2210/pdb9cxr/pdb |
| Descriptor | Poly(hexamethylene adipamide) hydrolase, 1,2-ETHANEDIOL, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | nylon oligomer, hydrolase |
| Biological source | Alphaproteobacteria bacterium |
| Total number of polymer chains | 2 |
| Total formula weight | 63126.00 |
| Authors | Meilleur, F.,Williams, A.N.,Drufva, E.E.,Parks, J.M.,Chen, S.H.,Michener, J.K. (deposition date: 2024-07-31, release date: 2025-01-29) |
| Primary citation | Drufva, E.E.,Cahill, J.F.,Saint-Vincent, P.M.B.,Williams, A.N.,Bocharova, V.,Capra, N.,Meilleur, F.,Carper, D.L.,Bourgery, C.,Miyazaki, K.,Yonemura, M.,Shiraishi, Y.,Parks, J.M.,Zhou, M.,Dishner, I.T.,Foster, J.C.,Koehler, S.J.,Valentino, H.R.,Sedova, A.,Kertesz, V.,Vasileva, D.P.,Hochanadel, L.H.,Figg, C.A.,Negoro, S.,Kato, D.I.,Chen, S.H.,Michener, J.K. Identification and characterization of substrate- and product-selective nylon hydrolases. Biorxiv, 2024 Cited by PubMed Abstract: Enzymes have evolved to rapidly and selectively hydrolyze diverse natural and anthropogenic polymers, but only a limited group of related enzymes have been shown to hydrolyze synthetic polyamides. In this work, we synthesized and characterized a panel of 95 diverse enzymes from the N-terminal nucleophile hydrolase superfamily with 30-50% pairwise amino acid identity. We found that nearly 40% of the enzymes had substantial nylon hydrolase activity, in many cases comparable to that of the best-characterized nylon hydrolase, NylC. There was no relationship between phylogeny and activity, nor any evidence of prior selection for nylon hydrolase activity. Several newly-identified hydrolases showed significant substrate selectivity, generating up to 20-fold higher product titers with Nylon 6,6 versus Nylon 6. Finally, we determined the crystal structure and oligomerization state of a Nylon 6,6-selective hydrolase to elucidate structural factors that could affect activity and selectivity. These new enzymes provide insights into the widespread potential for nylon hydrolase evolution and opportunities for analysis and engineering of improved hydrolases. PubMed: 39605696DOI: 10.1101/2024.11.14.623603 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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