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8AGQ

Crystal structure of anthocyanin-related GSTF8 from Populus trichocarpa in complex with (-)-catechin and glutathione

Summary for 8AGQ
Entry DOI10.2210/pdb8agq/pdb
DescriptorGlutathione 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 Keywordsanthocyanin, dehydratase, transferase
Biological sourcePopulus trichocarpa (black cottonwood)
Total number of polymer chains1
Total formula weight25170.69
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 citationEichenberger, 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: 37881531
DOI: 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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