9MGZ
Dunaliella tertiolecta PSI-LHCI-TIDI1 supercomplex
Summary for 9MGZ
| Entry DOI | 10.2210/pdb9mgz/pdb |
| Related | 9MGW |
| EMDB information | 48262 48264 |
| Descriptor | Chlorophyll a-b binding protein, chloroplastic, PSAF1, Photosystem I reaction center subunit IX, ... (30 entities in total) |
| Functional Keywords | iron homeostasis; membrane protein; photosystem i; dunaliella; green alga; psi-lhci supercomplex; tidi; thylakoid iron-deficiency induced protein; photosynthetic apparatus; photosynthesis; eukaryotes, photosynthesis; dunaliella tertiolecta, photosynthesis |
| Biological source | Dunaliella tertiolecta More |
| Total number of polymer chains | 18 |
| Total formula weight | 740885.50 |
| Authors | |
| Primary citation | Liu, H.W.,Khera, R.,Grob, P.,Gallaher, S.D.,Purvine, S.O.,Nicora, C.D.,Lipton, M.S.,Niyogi, K.K.,Nogales, E.,Iwai, M.,Merchant, S.S. A distinct LHCI arrangement is recruited to photosystem I in Fe-starved green algae. Proc.Natl.Acad.Sci.USA, 122:e2500621122-e2500621122, 2025 Cited by PubMed Abstract: Iron (Fe) availability limits photosynthesis at a global scale where Fe-rich photosystem (PS) I abundance is drastically reduced in Fe-poor environments. We used single-particle cryoelectron microscopy to reveal a unique Fe starvation-dependent arrangement of light-harvesting chlorophyll (LHC) proteins where Fe starvation-induced TIDI1 is found in an additional tetramer of LHC proteins associated with PSI in and . These cosmopolitan green algae are resilient to poor Fe nutrition. TIDI1 is a distinct LHC protein that co-occurs in diverse algae with flavodoxin (an Fe-independent replacement for the Fe-containing ferredoxin). The antenna expansion in eukaryotic algae we describe here is reminiscent of the iron-starvation induced (encoding) antenna ring in cyanobacteria, which typically co-occurs with , encoding flavodoxin. Our work showcases the convergent strategies that evolved after the Great Oxidation Event to maintain PSI capacity. PubMed: 40523173DOI: 10.1073/pnas.2500621122 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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