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9AU4

Cryo-EM structure of a photosystem I variant containing an unusual plastoquinone derivative in its electron transfer chain

This is a non-PDB format compatible entry.
Summary for 9AU4
Entry DOI10.2210/pdb9au4/pdb
EMDB information43843
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XI, Photosystem I reaction center subunit XII, ... (27 entities in total)
Functional Keywordscyanobacteria, photosystem i, menb, phylloquinone, plastoquinone, benzoquinone, naphthoquinone, redox potential, photosynthesis
Biological sourceSynechocystis sp. PCC 6803
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Total number of polymer chains33
Total formula weight1077744.42
Authors
Primary citationGisriel, C.J.,Kurashov, V.,Iwig, D.F.,Russell, B.P.,Vinyard, D.J.,Brudvig, G.W.,Golbeck, J.H.,Lakshmi, K.V.
Cryo-EM structure of a photosystem I variant containing an unusual plastoquinone derivative in its electron transfer chain.
Sci Adv, 10:eadp4937-eadp4937, 2024
Cited by
PubMed Abstract: Photosystem I (PS I) is a light-driven oxidoreductase responsible for converting photons into chemical bond energy. Its application for renewable energy was revolutionized by the creation of the MenB deletion (Δ) variant in the cyanobacterium sp. PCC 6803, in which phylloquinone is replaced by plastoquinone-9 with a low binding affinity. This permits its exchange with exogenous quinones covalently coupled to dihydrogen catalysts that bind with high affinity, thereby converting PS I into a stable solar fuel catalyst. Here, we reveal the 2.03-Å-resolution cryo-EM structure of a recent MenB variant of PS I. The quinones and their binding environment are analyzed in the context of previous biophysical data, thereby enabling a protocol to solve future PS I hybrids and constructs from this genetically tractable cyanobacterium.
PubMed: 39612342
DOI: 10.1126/sciadv.adp4937
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.03 Å)
Structure validation

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