7VWS

Carbazole Prenyl Transferase LvqB4

Summary for 7VWS

• Entry DOI: 10.2210/pdb7vws/pdb
• Descriptor: LvqB4, MAGNESIUM ION, 2-methyl-1-[(2R)-2-oxidanylpropyl]-9H-carbazole-3,4-dione, ... (5 entities in total)
• Functional Keywords: prenyl transferase, squalene synthase, transferase
• Biological source: Streptomyces sp.
• Total number of polymer chains: 2
• Total formula weight: 83320.92

Authors

Suemune, H.,Nagata, R.,Kuzuyama, T.,Nagano, S. (deposition date: 2021-11-11, release date: 2022-03-23, Last modification date: 2024-04-03)

Primary citation

Nagata, R.,Suemune, H.,Kobayashi, M.,Shinada, T.,Shin-Ya, K.,Nishiyama, M.,Hino, T.,Sato, Y.,Kuzuyama, T.,Nagano, S.
Structural Basis for the Prenylation Reaction of Carbazole-Containing Natural Products Catalyzed by Squalene Synthase-Like Enzymes.
Angew.Chem.Int.Ed.Engl., 61:e202117430-e202117430, 2022

PubMed Abstract: 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 σ-complex involving a catalytic triad is proposed. Our results provide a structural basis for a new subclass of aromatic substrate PTs.

PubMed: 35235232
DOI: 10.1002/anie.202117430

Experimental method

X-RAY DIFFRACTION (1.71 Å)