6A2W
Crystal structure of fucoxanthin chlorophyll a/c complex from Phaeodactylum tricornutum
Summary for 6A2W
| Entry DOI | 10.2210/pdb6a2w/pdb |
| Descriptor | Protein fucoxanthin chlorophyl a/c protein, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE, octyl 1-thio-beta-D-glucopyranoside, ... (13 entities in total) |
| Functional Keywords | photosynthesis, light-harvesting, fucoxanthin, diatom |
| Biological source | Phaeodactylum tricornutum CCAP 1055/1 |
| Total number of polymer chains | 1 |
| Total formula weight | 34509.09 |
| Authors | Wang, W.,Yu, L.J.,Kuang, T.Y.,Shen, J.R. (deposition date: 2018-06-13, release date: 2019-02-06, Last modification date: 2024-03-27) |
| Primary citation | Wang, W.,Yu, L.J.,Xu, C.,Tomizaki, T.,Zhao, S.,Umena, Y.,Chen, X.,Qin, X.,Xin, Y.,Suga, M.,Han, G.,Kuang, T.,Shen, J.R. Structural basis for blue-green light harvesting and energy dissipation in diatoms. Science, 363:-, 2019 Cited by PubMed Abstract: Diatoms 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 , 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. PubMed: 30733387DOI: 10.1126/science.aav0365 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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