WebOur X-ray crystal structures reveal that CylK is a distinctive fusion of Ca2+-binding and β-propeller domains, and site-directed mutagenesis and anomalous diffraction with bound bromide ions locate the active site to the domain interface. WebMay 26, 2024 · The overlay of the crystal structure with the co-crystallized ligand 2-azasqualene and the calculated binding mode of the geranyl phenyl ether show that 1 folds into the active pocket in the opposite direction to the 2-azasqualene. However, the double bond of the first isoprene units is positioned appropriately for initial protonation by the D376.
Structural Basis for the Friedel-Crafts Alkylation in ...
WebDec 2, 2024 · The cyanobacterial enzyme CylK assembles the cylindrocyclophane natural products by performing two unusual alkylation reactions, forming new … WebFeb 25, 2024 · Europe PMC is an archive of life sciences journal literature. dgsb facebook
Structural basis for an unprecedented enzymatic …
WebCylK is the key enzyme that catalyzes the formation of the cylindrocyclophane scaffold through the Friedel–Crafts alkylation reactions with regioselectivity and stereospecificity. Further research demonstrates that CylK can accept other resorcinol rings and secondary alkyl halides as substrates. WebCylindrocyclophanes were the first cyclophanes found in nature, isolated from a species of cyanobacteria, and have proven to be an interesting group of compounds to study due to their unusual molecular structure and intriguing biological possibilities, especially its cytotoxicity to some cancer cell lines. Contents 1 Origin 2 Structure WebFeb 25, 2024 · The CylK X-ray crystal structure reveals a distinct arrangement of two protein domains. ( A) An overall view of the structure of CylK. In this image and throughout, calcium ions are shown as blue spheres, magnesium ions as dark gray spheres, and chloride ions as green spheres. The … see more Figure 2—figure supplement 1 2+ 2+ … cicero in verrem gottwein