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6YAC

Plant PSI-ferredoxin supercomplex

Summary for 6YAC
Entry DOI10.2210/pdb6yac/pdb
Related5L8R
EMDB information10746
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit IX, Photosystem I reaction center subunit X psaK, ... (33 entities in total)
Functional Keywordsmembrane complex, photosystem i, ferredoxin, light harvesting, excitation transfer, photosynthesis
Biological sourcePisum sativum (Pea)
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Total number of polymer chains17
Total formula weight562539.25
Authors
Caspy, I.,Nelson, N.,Shkolnisky, Y.,Klaiman, D.,Sheinker, A. (deposition date: 2020-03-12, release date: 2020-09-30, Last modification date: 2020-10-21)
Primary citationCaspy, I.,Borovikova-Sheinker, A.,Klaiman, D.,Shkolnisky, Y.,Nelson, N.
The structure of a triple complex of plant photosystem I with ferredoxin and plastocyanin.
Nat.Plants, 6:1300-1305, 2020
Cited by
PubMed Abstract: The ability of photosynthetic organisms to use sunlight as a sole source of energy is endowed by two large membrane complexes-photosystem I (PSI) and photosystem II (PSII). PSI and PSII are the fundamental components of oxygenic photosynthesis, providing oxygen, food and an energy source for most living organisms on Earth. Currently, high-resolution crystal structures of these complexes from various organisms are available. The crystal structures of megadalton complexes have revealed excitation transfer and electron-transport pathways within the various complexes. PSI is defined as plastocyanin-ferredoxin oxidoreductase but a high-resolution structure of the entire triple supercomplex is not available. Here, using a new cryo-electron microscopy technique, we solve the structure of native plant PSI in complex with its electron donor plastocyanin and the electron acceptor ferredoxin. We reveal all of the contact sites and the modes of interaction between the interacting electron carriers and PSI.
PubMed: 33020607
DOI: 10.1038/s41477-020-00779-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.5 Å)
Structure validation

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