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| Title | Cryo-EM structural analyses of chlorophyll b-enriched PSI-LHC and PSII-LHC supercomplexes of the siphonous green alga Bryopsis corticulans. |
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| Journal, issue, pages | Plant Commun, Vol. 7, Issue 5, Page 101738, Year 2026 |
| Publish date | May 11, 2026 |
Authors | Xueyang Liu / Zhenhua Li / Liangliang Shen / Lili Shen / Bin Wu / Xiaoyi Li / Yanyan Yang / Shan Gao / Guangye Han / Tingyun Kuang / Cheng Liu / Jian-Ren Shen / Wenda Wang / ![]() |
| PubMed Abstract | The light-harvesting complexes of photosystem I (PSI) and PSII (LHCI and LHCII) in Bryopsis corticulans (B. corticulans) are homologous to those in Chlamydomonas reinhardtii and land plants but ...The light-harvesting complexes of photosystem I (PSI) and PSII (LHCI and LHCII) in Bryopsis corticulans (B. corticulans) are homologous to those in Chlamydomonas reinhardtii and land plants but exhibit a distinct chlorophyll (Chl) and carotenoid composition. Here, we report cryo-electron microscopy structures of the PSI-LHCI-LHCII supercomplex, comprising three LHCII trimers, and the CSMN-type PSII-LHCII supercomplex from B. corticulans. In the PSI supercomplex, ten LHCI subunits assemble into two belts and one heterodimer, coordinating a total of 86 Chl a and 65 Chl b molecules (Chl a/b ratio of 1.3, compared with 3.4 in C. reinhardtii), as well as 18 siphonaxanthin, 2 siphonein, and 13 α-carotene molecules. Of the three LHCII trimers bound to the PSI-LHCI supercomplex, two are anchored to the PSI core primarily via phosphorylated subunits, whereas the third, non-phosphorylated trimer is stabilized through interactions with Lhca-d and the adjacent LHCII trimer. In the CSMN-type PSII-LHCII supercomplex, the N-LHCII is positioned closer to the PSII core than in C. reinhardtii, likely owing to loss of the linker motif in the N-terminal region of B. corticulans CP29. Structure-based energy transfer analysis suggests that this spatial rearrangement enhances the efficiency of excitation energy transfer from N-LHCII to the PSII core. Collectively, these findings reveal structural adaptations that underlie the acclimation strategies of siphonous green algae inhabiting intertidal environments. |
External links | Plant Commun / PubMed:41578646 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.68 - 3.07 Å |
| Structure data | EMDB-61940, PDB-9jzr: EMDB-61973, PDB-9k1e: EMDB-62153, PDB-9k7v: |
| Chemicals | ![]() ChemComp-CHL: ![]() ChemComp-CLA: ![]() ChemComp-8CT: ![]() ChemComp-0UR: ![]() ChemComp-LHG: ![]() ChemComp-SQD: ![]() ChemComp-LMG: ![]() ChemComp-0IE: ![]() ChemComp-PQN: ![]() ChemComp-CL0: ![]() ChemComp-SF4: ![]() ChemComp-DGD: ![]() ChemComp-NEX: ![]() ChemComp-HEM: ![]() ChemComp-XAT: ![]() ChemComp-OEX: ![]() ChemComp-PHO: ![]() ChemComp-BCT: ![]() ChemComp-FE2: ![]() ChemComp-PL9: |
| Source |
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Keywords | PHOTOSYNTHESIS / photosystem II / PSI-LHCI supercomplex / PSII-LHCII supercomplex |
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bryopsis corticulans (plant)
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