9dys

X-ray Crystallographic Structure of the Poly(Hexamethylene Adipamide) (Nylon66) Hydrolase Nyl50 at Room Temperature bound to tetraethylene glycol

spinqualitylabelsall models 9dys, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9dys is a 2 chain structure with sequence from Alphaproteobacteria bacterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: EDO, NA, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A522DD61_9PROT Publication Abstract from PubMed 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. Identification and characterization of substrate- and product-selective nylon hydrolases.,Drufva EE, Cahill JF, Saint-Vincent PMB, Williams AN, Bocharova V, Capra N, Meilleur F, Carper DL, Bourgery C, Miyazaki K, Yonemura M, Shiraishi Y, Parks JM, Zhou M, Dishner IT, Foster JC, Koehler SJ, Valentino HR, Sedova A, Kertesz V, Vasileva DP, Hochanadel LH, Figg CA, Negoro S, Kato DI, Chen SH, Michener JK bioRxiv [Preprint]. 2024 Nov 14:2024.11.14.623603. doi: , 10.1101/2024.11.14.623603. PMID:39605696 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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