8HW1
Far-red light-harvesting complex of Antarctic alga Prasiola crispa
Summary for 8HW1
| Entry DOI | 10.2210/pdb8hw1/pdb |
| EMDB information | 35080 |
| Descriptor | Far-red light-harvesting complex, CHLOROPHYLL A, (3S,5R,6S,3'S,5'R,6'S)-5,6,5',6'-DIEPOXY-5,6,5',6'- TETRAHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL, ... (4 entities in total) |
| Functional Keywords | undecameric ring, light-harvesting complex, photosynthesis |
| Biological source | Prasiola crispa |
| Total number of polymer chains | 11 |
| Total formula weight | 489606.00 |
| Authors | Kosugi, M.,Kawasaki, M.,Shibata, Y.,Moriya, T.,Adachi, N.,Senda, T. (deposition date: 2022-12-28, release date: 2023-01-18, Last modification date: 2024-07-03) |
| Primary citation | Kosugi, M.,Kawasaki, M.,Shibata, Y.,Hara, K.,Takaichi, S.,Moriya, T.,Adachi, N.,Kamei, Y.,Kashino, Y.,Kudoh, S.,Koike, H.,Senda, T. Uphill energy transfer mechanism for photosynthesis in an Antarctic alga. Nat Commun, 14:730-730, 2023 Cited by PubMed Abstract: Prasiola crispa, an aerial green alga, forms layered colonies under the severe terrestrial conditions of Antarctica. Since only far-red light is available at a deep layer of the colony, P. crispa has evolved a molecular system for photosystem II (PSII) excitation using far-red light with uphill energy transfer. However, the molecular basis underlying this system remains elusive. Here, we purified a light-harvesting chlorophyll (Chl)-binding protein complex from P. crispa (Pc-frLHC) that excites PSII with far-red light and revealed its ring-shaped structure with undecameric 11-fold symmetry at 3.13 Å resolution. The primary structure suggests that Pc-frLHC evolved from LHCI rather than LHCII. The circular arrangement of the Pc-frLHC subunits is unique among eukaryote LHCs and forms unprecedented Chl pentamers at every subunit‒subunit interface near the excitation energy exit sites. The Chl pentamers probably contribute to far-red light absorption. Pc-frLHC's unique Chl arrangement likely promotes PSII excitation with entropy-driven uphill excitation energy transfer. PubMed: 36792917DOI: 10.1038/s41467-023-36245-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.13 Å) |
Structure validation
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