8AGQ
Crystal structure of anthocyanin-related GSTF8 from Populus trichocarpa in complex with (-)-catechin and glutathione
Summary for 8AGQ
Entry DOI | 10.2210/pdb8agq/pdb |
Descriptor | Glutathione transferase, GLUTATHIONE, (2~{S},3~{R})-2-[3,4-bis(oxidanyl)phenyl]-3,4-dihydro-2~{H}-chromene-3,5,7-triol, ... (5 entities in total) |
Functional Keywords | anthocyanin, dehydratase, transferase |
Biological source | Populus trichocarpa (black cottonwood) |
Total number of polymer chains | 1 |
Total formula weight | 25170.69 |
Authors | Eichenberger, M.,Hueppi, S.,Schwander, T.,Mittl, P.,Buller, M.R. (deposition date: 2022-07-20, release date: 2023-08-30, Last modification date: 2023-11-08) |
Primary citation | Eichenberger, M.,Schwander, T.,Huppi, S.,Kreuzer, J.,Mittl, P.R.E.,Peccati, F.,Jimenez-Oses, G.,Naesby, M.,Buller, R.M. The catalytic role of glutathione transferases in heterologous anthocyanin biosynthesis. Nat Catal, 6:927-938, 2023 Cited by PubMed Abstract: Anthocyanins are ubiquitous plant pigments used in a variety of technological applications. Yet, after over a century of research, the penultimate biosynthetic step to anthocyanidins attributed to the action of leucoanthocyanidin dioxygenase has never been efficiently reconstituted outside plants, preventing the construction of heterologous cell factories. Through biochemical and structural analysis, here we show that anthocyanin-related glutathione transferases, currently implicated only in anthocyanin transport, catalyse an essential dehydration of the leucoanthocyanidin dioxygenase product, flavan-3,3,4-triol, to generate cyanidin. Building on this knowledge, introduction of anthocyanin-related glutathione transferases into a heterologous biosynthetic pathway in baker's yeast results in >35-fold increased anthocyanin production. In addition to unravelling the long-elusive anthocyanin biosynthesis, our findings pave the way for the colourants' heterologous microbial production and could impact the breeding of industrial and ornamental plants. PubMed: 37881531DOI: 10.1038/s41929-023-01018-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.093 Å) |
Structure validation
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