8DDY
Helical rods of far-red light-absorbing allophycocyanin in Synechococcus sp.
Summary for 8DDY
| Entry DOI | 10.2210/pdb8ddy/pdb |
| EMDB information | 27382 |
| Descriptor | Allophycocyanin subunit alpha, Allophycocyanin subunit beta, PHYCOCYANOBILIN, ... (5 entities in total) |
| Functional Keywords | allophycocyanin, phycobiliprotein, photosystem, photosynthesis, energy transfer, cyanobacteria, far-red light, farlip, lolip |
| Biological source | Synechococcus sp. 63AY4M1 More |
| Total number of polymer chains | 6 |
| Total formula weight | 118354.99 |
| Authors | Gisriel, C.J.,Shen, G.S.,Soulier, N.T.,Flesher, D.A.,Brudvig, G.W.,Bryant, D.A. (deposition date: 2022-06-19, release date: 2023-04-05) |
| Primary citation | Gisriel, C.J.,Elias, E.,Shen, G.,Soulier, N.T.,Flesher, D.A.,Gunner, M.R.,Brudvig, G.W.,Croce, R.,Bryant, D.A. Helical allophycocyanin nanotubes absorb far-red light in a thermophilic cyanobacterium. Sci Adv, 9:eadg0251-eadg0251, 2023 Cited by PubMed Abstract: To compete in certain low-light environments, some cyanobacteria express a paralog of the light-harvesting phycobiliprotein, allophycocyanin (AP), that strongly absorbs far-red light (FRL). Using cryo-electron microscopy and time-resolved absorption spectroscopy, we reveal the structure-function relationship of this FRL-absorbing AP complex (FRL-AP) that is expressed during acclimation to low light and that likely associates with chlorophyll a-containing photosystem I. FRL-AP assembles as helical nanotubes rather than typical toroids due to alterations of the domain geometry within each subunit. Spectroscopic characterization suggests that FRL-AP nanotubes are somewhat inefficient antenna; however, the enhanced ability to harvest FRL when visible light is severely attenuated represents a beneficial trade-off. The results expand the known diversity of light-harvesting proteins in nature and exemplify how biological plasticity is achieved by balancing resource accessibility with efficiency. PubMed: 36961897DOI: 10.1126/sciadv.adg0251 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.89 Å) |
Structure validation
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