9W1C
LH2 complex from Ectothiorhodospira haloalkaliphila with inhibited carotenoid biosynthesis
This is a non-PDB format compatible entry.
Summary for 9W1C
| Entry DOI | 10.2210/pdb9w1c/pdb |
| EMDB information | 65526 |
| Descriptor | Light-harvesting protein B:800-850 subunit beta, Light-harvesting protein B-800/850 alpha chain, BACTERIOCHLOROPHYLL A, ... (5 entities in total) |
| Functional Keywords | photosynthesis, light-harvesing, purple sulfur bacteria, cryo-em |
| Biological source | Ectothiorhodospira haloalkaliphila ATCC 51935 More |
| Total number of polymer chains | 16 |
| Total formula weight | 132828.70 |
| Authors | Burtseva, A.D.,Baymukhametov, T.N.,Popov, V.O.,Ashikhmin, A.A.,Boyko, K.M. (deposition date: 2025-07-25, release date: 2025-10-22, Last modification date: 2025-12-10) |
| Primary citation | Burtseva, A.D.,Baymukhametov, T.N.,Bolshakov, M.A.,Starodubov, A.S.,Zhang, H.,Popov, V.O.,Ashikhmin, A.A.,Boyko, K.M. Structural insights into LH2 complexes formed by a purple sulfur bacterium with inhibited carotenoid biosynthesis. Febs Lett., 2025 Cited by PubMed Abstract: The LH2 complex is essential for light harvesting in many photosynthetic bacteria. To elucidate the specific structural role of carotenoids, we analyzed LH2 complexes from Ectothiorhodospira haloalkaliphila with inhibited carotenoid biosynthesis. This approach allowed us to study complexes incorporating the colorless carotenoid phytoene instead of the native, colored pigments. A 1.92 Å cryo-EM reconstruction revealed that phytoene fully substitutes for the native carotenoids while maintaining the octameric symmetry of the complex and the precise arrangement of bacteriochlorophylls. These results demonstrate that the architectural function of carotenoids in LH2 complexes is maintained even when their light-absorption capability is altered, providing new mechanistic insight into the structural basis of pigment-protein interactions in photosynthetic antenna complexes. PubMed: 41313718DOI: 10.1002/1873-3468.70242 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.92 Å) |
Structure validation
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