9LT4
Cryo-EM structure of light harvesting complex 2 from Ery. sanguineus
This is a non-PDB format compatible entry.
Summary for 9LT4
| Entry DOI | 10.2210/pdb9lt4/pdb |
| EMDB information | 63365 |
| Descriptor | Light-harvesting protein B-800/814 alpha chain, Light-harvesting protein B-800-850 beta chain, BACTERIOCHLOROPHYLL A, ... (4 entities in total) |
| Functional Keywords | light harvesting complex 2, erythrobacte sanguineus, photosynthesis |
| Biological source | Erythrobacter sanguineus More |
| Total number of polymer chains | 18 |
| Total formula weight | 145964.15 |
| Authors | Yue, X.-Y.,Wang, G.-L.,Yu, L.-J. (deposition date: 2025-02-05, release date: 2025-12-10, Last modification date: 2026-02-25) |
| Primary citation | Yue, X.Y.,Wang, G.L.,Zou, M.J.,Ma, F.,Wang-Otomo, Z.Y.,Madigan, M.T.,Yu, L.J. Cryo-EM structures of photocomplexes from the free-living aerobic anoxygenic phototrophic bacterium Erythrobacter sanguineus. Structure, 34:334-, 2026 Cited by PubMed Abstract: Aerobic anoxygenic phototrophic bacteria (AAPB) are widely distributed in nature and they are important members of the marine phototrophic community. However, a structural and functional understanding of the AAPB photosynthetic apparatus is still lacking. Here, we present cryo-EM structures of the LH1-RC (core) and LH2 (peripheral) photocomplexes from the model aerobic phototroph Erythrobacter (Ery.) sanguineus. The LH1 αβ-heterodimers bind the carotenoids bacteriorubixanthinal and caloxanthin-pigments that are absent from anaerobic anoxygenic phototrophs-to form a closed ring structure. Ery. sanguineus LH1-RC contains a lipid-anchored polypeptide unrelated to any of the auxiliary proteins identified in the core complexes of purple bacteria so far. The Ery. sanguineus LH2 complex shows unique absorption characteristics, with its Q transition being blue-shifted to 814 nm. This work provides structural insights into the unusual photosynthetic properties of AAPB and points to new avenues to further explore their biology. PubMed: 41274286DOI: 10.1016/j.str.2025.10.017 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.74 Å) |
Structure validation
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