TY - JOUR
T1 - Structural basis for blue-green light harvesting and energy dissipation in diatoms
AU - Wang, Wenda
AU - Yu, Long Jiang
AU - Xu, Caizhe
AU - Tomizaki, Takashi
AU - Zhao, Songhao
AU - Umena, Yasufumi
AU - Chen, Xiaobo
AU - Qin, Xiaochun
AU - Xin, Yueyong
AU - Suga, Michihiro
AU - Han, Guangye
AU - Kuang, Tingyun
AU - Shen, Jian Ren
N1 - Funding Information:
We thank M. Sang and D. Chen for their help with the culture of the diatom cells, N. Matsugaki for help on the collection of the SAD data, the CCP4 workshop team (SPring-8 Japan, 2017) for advices on analyzing the native-SAD data and phasing, and H. Lin for discussions. Diffraction data at 1.0-Å wavelength was collected at beamlines BL17U1 of Shanghai Synchrotron Radiation Facility (SSRF, China) and BL41XU of SPring-8 (Japan); Native SAD data was collected at beamlines BL1A of Photon Factory (PF, Japan) and X06DA of Swiss Light Source at the Paul Scherrer Institute, and we thank the staff members of these beamlines for their extensive support. This work was supported by the National Key R&D Program of China (2017YFA0503700), a Strategic Priority Research Program of CAS (XDB17000000), a CAS Key Research program for Frontier Science (QYZDY-SSW-SMC003), a National Basic Research Program of China (2015CB150100 to T.K.), and JSPS KAKENHI no. JP17H0643419 of MEXT, Japan (to J.-R.S.).
PY - 2019/2/8
Y1 - 2019/2/8
N2 - 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 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.
AB - 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 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.
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U2 - 10.1126/science.aav0365
DO - 10.1126/science.aav0365
M3 - Article
C2 - 30733387
AN - SCOPUS:85061204092
VL - 363
JO - Science
JF - Science
SN - 0036-8075
IS - 6427
ER -
