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6K33

Structure of PSI-isiA supercomplex from Thermosynechococcus vulcanus

This is a non-PDB format compatible entry.
Summary for 6K33
Entry DOI10.2210/pdb6k33/pdb
EMDB information9908
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XI, Photosystem I reaction center subunit XII, ... (22 entities in total)
Functional Keywordselectron transport, photosynthesis
Biological sourceThermosynechococcus vulcanus
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Total number of polymer chains54
Total formula weight2096200.88
Authors
Akita, F.,Nagao, R.,Kato, K.,Shen, J.R.,Miyazaki, N. (deposition date: 2019-05-16, release date: 2020-05-20, Last modification date: 2024-10-16)
Primary citationAkita, F.,Nagao, R.,Kato, K.,Nakajima, Y.,Yokono, M.,Ueno, Y.,Suzuki, T.,Dohmae, N.,Shen, J.R.,Akimoto, S.,Miyazaki, N.
Structure of a cyanobacterial photosystem I surrounded by octadecameric IsiA antenna proteins.
Commun Biol, 3:232-232, 2020
Cited by
PubMed Abstract: Iron-stress induced protein A (IsiA) is a chlorophyll-binding membrane-spanning protein in photosynthetic prokaryote cyanobacteria, and is associated with photosystem I (PSI) trimer cores, but its structural and functional significance in light harvesting remains unclear. Here we report a 2.7-Å resolution cryo-electron microscopic structure of a supercomplex between PSI core trimer and IsiA from a thermophilic cyanobacterium Thermosynechococcus vulcanus. The structure showed that 18 IsiA subunits form a closed ring surrounding a PSI trimer core. Detailed arrangement of pigments within the supercomplex, as well as molecular interactions between PSI and IsiA and among IsiAs, were resolved. Time-resolved fluorescence spectra of the PSI-IsiA supercomplex showed clear excitation-energy transfer from IsiA to PSI, strongly indicating that IsiA functions as an energy donor, but not an energy quencher, in the supercomplex. These structural and spectroscopic findings provide important insights into the excitation-energy-transfer and subunit assembly mechanisms in the PSI-IsiA supercomplex.
PubMed: 32393811
DOI: 10.1038/s42003-020-0949-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.74 Å)
Structure validation

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