7Y3F
Structure of the Anabaena PSI-monomer-IsiA supercomplex
Summary for 7Y3F
| Entry DOI | 10.2210/pdb7y3f/pdb |
| EMDB information | 33593 |
| Descriptor | Photosystem I P700 chlorophyll a apoprotein A1, PsaM, Photosystem I 4.8 kDa protein, ... (23 entities in total) |
| Functional Keywords | photosystem i, electron transport, isia, photosynthesis |
| Biological source | Nostoc sp. More |
| Total number of polymer chains | 17 |
| Total formula weight | 617159.68 |
| Authors | Nagao, R.,Kato, K.,Hamaguchi, T.,Kawakami, K.,Yonekura, K.,Shen, J.R. (deposition date: 2022-06-10, release date: 2023-03-01, Last modification date: 2024-10-23) |
| Primary citation | Nagao, R.,Kato, K.,Hamaguchi, T.,Ueno, Y.,Tsuboshita, N.,Shimizu, S.,Furutani, M.,Ehira, S.,Nakajima, Y.,Kawakami, K.,Suzuki, T.,Dohmae, N.,Akimoto, S.,Yonekura, K.,Shen, J.R. Structure of a monomeric photosystem I core associated with iron-stress-induced-A proteins from Anabaena sp. PCC 7120. Nat Commun, 14:920-920, 2023 Cited by PubMed Abstract: Iron-stress-induced-A proteins (IsiAs) are expressed in cyanobacteria under iron-deficient conditions. The cyanobacterium Anabaena sp. PCC 7120 has four isiA genes; however, their binding property and functional roles in PSI are still missing. We analyzed a cryo-electron microscopy structure of a PSI-IsiA supercomplex isolated from Anabaena grown under an iron-deficient condition. The PSI-IsiA structure contains six IsiA subunits associated with the PsaA side of a PSI core monomer. Three of the six IsiA subunits were identified as IsiA1 and IsiA2. The PSI-IsiA structure lacks a PsaL subunit; instead, a C-terminal domain of IsiA2 occupies the position of PsaL, which inhibits the oligomerization of PSI, leading to the formation of a PSI monomer. Furthermore, excitation-energy transfer from IsiAs to PSI appeared with a time constant of 55 ps. These findings provide insights into both the molecular assembly of the Anabaena IsiA family and the functional roles of IsiAs. PubMed: 36805598DOI: 10.1038/s41467-023-36504-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.62 Å) |
Structure validation
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