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9LZJ

The PSI3-IsiA43 complex with a closed double ring of IsiA proteins bound to a trimeric PSI core

This is a non-PDB format compatible entry.
Summary for 9LZJ
Entry DOI10.2210/pdb9lzj/pdb
Related9LZK
EMDB information63527
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XI, Photosystem I reaction center subunit XII, ... (22 entities in total)
Functional Keywordsphotosystem-antenna complex, photosynthesis
Biological sourceThermosynechococcus vestitus BP-1
More
Total number of polymer chains79
Total formula weight3566278.10
Authors
Si, L.,Cao, P.,Li, M. (deposition date: 2025-02-21, release date: 2025-12-31, Last modification date: 2026-01-28)
Primary citationSi, L.,Zhang, Y.,Su, X.,Zhao, X.,An, X.,Liu, L.N.,Cao, P.,Li, M.
Structural basis for the assembly and energy transfer between the cyanobacterial PSI core and the double-layered IsiA proteins.
Nat Commun, 17:592-592, 2025
Cited by
PubMed Abstract: Iron-limitation is a common stress factor in natural environments. To survive under iron-starved conditions, cyanobacteria overexpress iron stress-induced protein A (IsiA), which is crucial for light-harvesting and photoprotection. Multiple IsiA proteins form a single- or double-layered architecture encircling the photosystem I (PSI) core, forming various PSI-IsiA supercomplexes. The assembly and energy transfer mechanisms of double-layered PSI-IsiA supercomplexes remain unelucidated. Here, we present high-resolution structures of two PSI-IsiA supercomplexes isolated from the cyanobacterium Thermosynechococcus elongatus BP-1 cultured under iron-starved conditions. The PSI-IsiA complex contains a trimeric PSI core surrounded by 43 IsiA subunits assembled into a closed double-ring. The PSI-IsiA complex contains 13 IsiA proteins arranged in a double-layered architecture attached to the monomeric PSI core. Atomic force microscopy demonstrates the presence and distribution of different PSI-IsiA complexes within native thylakoid membranes isolated from iron-starved cells. Our findings provide insights into the structural variability and adaptive mechanisms of PSI-IsiA complexes.
PubMed: 41422266
DOI: 10.1038/s41467-025-67295-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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