7vws | pdb_00007vws

Carbazole Prenyl Transferase LvqB4

spinqualitylabelsall models 7vws, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7vws is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 83B, AO6, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Some enzymes annotated as squalene synthase catalyze the prenylation of carbazole-3,4-quinone-containing substrates in bacterial secondary metabolism. Their reaction mechanisms remain unclear because of their low sequence similarity to well-characterized aromatic substrate prenyltransferases (PTs). We determined the crystal structures of the carbazole PTs, and these revealed that the overall structure is well superposed on those of squalene synthases. In contrast, the stacking interaction between the prenyl donor and acceptor substrates resembles those observed in aromatic substrate PTs. Structural and mutational analyses suggest that the Ile and Asp residues are essential for the hydrophobic and hydrophilic interactions with the carbazole-3,4-quinone moiety of the prenyl acceptor, respectively, and a deprotonation mechanism of an intermediary sigma-complex involving a catalytic triad is proposed. Our results provide a structural basis for a new subclass of aromatic substrate PTs. Structural Basis for the Prenylation Reaction of Carbazole-Containing Natural Products Catalyzed by Squalene Synthase-Like Enzymes.,Nagata R, Suemune H, Kobayashi M, Shinada T, Shin-Ya K, Nishiyama M, Hino T, Sato Y, Kuzuyama T, Nagano S Angew Chem Int Ed Engl. 2022 Mar 2:e202117430. doi: 10.1002/anie.202117430. PMID:35235232 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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