7S5L

Cembrene A synthase from Eleutherobia rubra

Summary for 7S5L

• Entry DOI: 10.2210/pdb7s5l/pdb
• Descriptor: Cembrene A synthase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: terpene, diterpene synthase, octocoral, cembrene a, eleutherobia rubra, biosynthetic protein
• Biological source: Eleutherobia rubra
• Total number of polymer chains: 1
• Total formula weight: 45982.49

Authors

Chen, P.Y.-T.,Moore, B.S. (deposition date: 2021-09-10, release date: 2022-06-08, Last modification date: 2024-05-22)

Primary citation

Burkhardt, I.,de Rond, T.,Chen, P.Y.,Moore, B.S.
Ancient plant-like terpene biosynthesis in corals.
Nat.Chem.Biol., 18:664-669, 2022

PubMed Abstract: Octocorals are major contributors of terpenoid chemical diversity in the ocean. Natural products from other sessile marine animals are primarily biosynthesized by symbiotic microbes rather than by the host. Here, we challenge this long-standing paradigm by describing a monophyletic lineage of animal-encoded terpene cyclases (TCs) ubiquitous in octocorals. We characterized 15 TC enzymes from nine genera, several of which produce precursors of iconic coral-specific terpenoids, such as pseudopterosin, lophotoxin and eleutherobin. X-ray crystallography revealed that coral TCs share conserved active site residues and structural features with bacterial TCs. The identification of coral TCs enabled the targeted identification of the enzyme that constructs the coral-exclusive capnellane scaffold. Several TC genes are colocalized with genes that encode enzymes known to modify terpenes. This work presents an example of biosynthetic capacity in the kingdom Animalia that rivals the chemical complexity generated by plants, unlocking the biotechnological potential of octocorals for biomedical applications.

PubMed: 35606558
DOI: 10.1038/s41589-022-01026-2

Experimental method

X-RAY DIFFRACTION (1.58 Å)