9P1O
Crystal structure of TCZ9 bound with Cannabigerolic acid (CBGA)
This is a non-PDB format compatible entry.
Summary for 9P1O
| Entry DOI | 10.2210/pdb9p1o/pdb |
| Descriptor | FAD-binding oxidoreductase, FLAVIN-ADENINE DINUCLEOTIDE, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | bbe-like enzyme flavoprotein bound with it's substrate cbga., flavoprotein |
| Biological source | Streptomyces sp. AJS327 |
| Total number of polymer chains | 1 |
| Total formula weight | 52950.85 |
| Authors | Sirohi, H.V.,Kao, Y.C.,Chang, G. (deposition date: 2025-06-10, release date: 2026-06-17, Last modification date: 2026-07-22) |
| Primary citation | Love, A.C.,Sirohi, H.,Hubert, F.M.,Kao, Y.C.,Quinnell, D.E.,Lan, T.,Gappy, R.,Sheehy, M.,Hsu, J.,Lee, A.,Zangwill, L.,Chang, T.,Palfey, B.A.,Chang, G.,Moore, B.S. Structural and biochemical basis for cannabinoid cyclase activity in marine bacterial flavoenzymes. Nat.Chem.Biol., 2026 Cited by PubMed Abstract: The marine bacterial flavoenzymes Clz9 and Tcz9 can process cannabigerolic acid to the minor cannabinoid, cannabichromenic acid (CBCA); however, the mechanistic details of this extrinsic transformation are still obscure. Here we report a thorough analysis of CBCA formation by Clz9 and Tcz9 through high-resolution crystallographic characterization, biochemical analysis and spectroscopic interrogation. Our work reveals that Clz9 and Tcz9 use different biochemical mechanisms from Cannabis cyclases and each other in their production of CBCA. Collection of a high-resolution substrate-bound structure provides additional key insights into how active site architecture affects substrate binding and stereoselectivity. Engineering approaches improve the stereoselectivity of CBCA formation by Clz9 and Tcz9, providing access to (R) and (S)-CBCA. Collectively, our work advances understanding of enzymatic cannabinoid formation and cements Clz9 and Tcz9 as two unique members of the BBE-like enzyme family with encouraging potential for biocatalytic cannabinoid production applications. PubMed: 42414636DOI: 10.1038/s41589-026-02257-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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