8HQ8
Bry-LHCII homotrimer of Bryopsis corticulans
8HQ8 の概要
エントリーDOI | 10.2210/pdb8hq8/pdb |
分子名称 | siphonaxanthin chlorophyll a/b binding light-harvesting complex II, Bry-Lhcb1, TRIMETHYL GLYCINE, 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE, ... (12 entities in total) |
機能のキーワード | light-harvesting complexes, siphonaxanthin, siphonein, photosynthesis |
由来する生物種 | Bryopsis corticulans |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 261922.48 |
構造登録者 | |
主引用文献 | Li, Z.,Zhou, C.,Zhao, S.,Zhang, J.,Liu, X.,Sang, M.,Qin, X.,Yang, Y.,Han, G.,Kuang, T.,Shen, J.R.,Wang, W. Structural and functional properties of different types of siphonous LHCII trimers from an intertidal green alga Bryopsis corticulans. Structure, 31:1247-1258.e3, 2023 Cited by PubMed Abstract: Light-harvesting complexes of photosystem II (LHCIIs) in green algae and plants are vital antenna apparatus for light harvesting, energy transfer, and photoprotection. Here we determined the structure of a siphonous-type LHCII trimer from the intertidal green alga Bryopsis corticulans by X-ray crystallography and cryo-electron microscopy (cryo-EM), and analyzed its functional properties by spectral analysis. The Bryopsis LHCII (Bry-LHCII) structures in both homotrimeric and heterotrimeric form show that green light-absorbing siphonaxanthin and siphonein occupied the sites of lutein and violaxanthin in plant LHCII, and two extra chlorophylls (Chls) b replaced Chls a. Binding of these pigments expands the blue-green light absorption of B. corticulans in the tidal zone. We observed differences between the Bry-LHCII homotrimer crystal and cryo-EM structures, and also between Bry-LHCII homotrimer and heterotrimer cryo-EM structures. These conformational changes may reflect the flexibility of Bry-LHCII, which may be required to adapt to light fluctuations from tidal rhythms. PubMed: 37633266DOI: 10.1016/j.str.2023.08.001 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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