8PZK
Crystal structure of the Orange Carotenoid Protein 2 (OCP2) from Gloeocapsa sp. PCC 7428
Summary for 8PZK
| Entry DOI | 10.2210/pdb8pzk/pdb |
| Descriptor | Orange carotenoid-binding protein, beta,beta-caroten-4-one, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total) |
| Functional Keywords | photoprotective protein, photosensory protein, ocp2, carotenoid binding, photosynthesis |
| Biological source | Gloeocapsa sp. PCC 7428 |
| Total number of polymer chains | 1 |
| Total formula weight | 36394.42 |
| Authors | Boyko, K.M.,Varfolomeeva, L.A.,Slonimskiy, Y.B.,Maksimov, E.G.,Popov, V.O.,Sluchanko, N.N. (deposition date: 2023-07-27, release date: 2024-01-03, Last modification date: 2024-10-09) |
| Primary citation | Sluchanko, N.N.,Maksimov, E.G.,Slonimskiy, Y.B.,Varfolomeeva, L.A.,Bukhanko, A.Y.,Egorkin, N.A.,Tsoraev, G.V.,Khrenova, M.G.,Ge, B.,Qin, S.,Boyko, K.M.,Popov, V.O. Structural framework for the understanding spectroscopic and functional signatures of the cyanobacterial Orange Carotenoid Protein families. Int.J.Biol.Macromol., 254:127874-127874, 2024 Cited by PubMed Abstract: The Orange Carotenoid Protein (OCP) is a unique photoreceptor crucial for cyanobacterial photoprotection. Best studied Synechocystis sp. PCC 6803 OCP belongs to the large OCP1 family. Downregulated by the Fluorescence Recovery Protein (FRP) in low-light, high-light-activated OCP1 binds to the phycobilisomes and performs non-photochemical quenching. Recently discovered families OCP2 and OCP3 remain structurally and functionally underexplored, and no systematic comparative studies have ever been conducted. Here we present two first crystal structures of OCP2 from morphoecophysiologically different cyanobacteria and provide their comprehensive structural, spectroscopic and functional comparison with OCP1, the recently described OCP3 and all-OCP ancestor. Structures enable correlation of spectroscopic signatures with the effective number of hydrogen and discovered here chalcogen bonds anchoring the ketocarotenoid in OCP, as well as with the rotation of the echinenone's β-ionone ring in the CTD. Structural data also helped rationalize the observed differences in OCP/FRP and OCP/phycobilisome functional interactions. These data are expected to foster OCP research and applications in optogenetics, targeted carotenoid delivery and cyanobacterial biomass engineering. PubMed: 37939760DOI: 10.1016/j.ijbiomac.2023.127874 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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