6a2w
From Proteopedia
Jump to navigationJump to search
Crystal structure of fucoxanthin chlorophyll a/c complex from Phaeodactylum tricornutum
| ||||||||||||
Structural highlights
FunctionPublication Abstract from PubMedDiatoms are abundant photosynthetic organisms in aquatic environments and contribute 40% of its primary productivity. An important factor that contributes to the success of diatoms is their fucoxanthin chlorophyll a/c-binding proteins (FCPs), which have exceptional light-harvesting and photoprotection capabilities. Here, we report the crystal structure of an FCP from the marine diatom Phaeodactylum tricornutum, which reveals the binding of seven chlorophylls (Chls) a, two Chls c, seven fucoxanthins (Fxs), and probably one diadinoxanthin within the protein scaffold. Efficient energy transfer pathways can be found between Chl a and c, and each Fx is surrounded by Chls, enabling the energy transfer and quenching via Fx highly efficient. The structure provides a basis for elucidating the mechanisms of blue-green light harvesting, energy transfer, and dissipation in diatoms. Structural basis for blue-green light harvesting and energy dissipation in diatoms.,Wang W, Yu LJ, Xu C, Tomizaki T, Zhao S, Umena Y, Chen X, Qin X, Xin Y, Suga M, Han G, Kuang T, Shen JR Science. 2019 Feb 8;363(6427). pii: 363/6427/eaav0365. doi:, 10.1126/science.aav0365. PMID:30733387[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 12:57, 13 August 2026.