8HQ8
Bry-LHCII homotrimer of Bryopsis corticulans
Summary for 8HQ8
Entry DOI | 10.2210/pdb8hq8/pdb |
Descriptor | siphonaxanthin chlorophyll a/b binding light-harvesting complex II, Bry-Lhcb1, TRIMETHYL GLYCINE, 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE, ... (12 entities in total) |
Functional Keywords | light-harvesting complexes, siphonaxanthin, siphonein, photosynthesis |
Biological source | Bryopsis corticulans |
Total number of polymer chains | 6 |
Total formula weight | 261922.48 |
Authors | Li, Z.H.,Shen, J.R.,Wang, W.D. (deposition date: 2022-12-13, release date: 2023-09-06, Last modification date: 2023-11-15) |
Primary citation | 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 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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