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4L6V

Crystal structure of a virus like photosystem I from the cyanobacterium Synechocystis PCC 6803

Summary for 4L6V
Entry DOI10.2210/pdb4l6v/pdb
Related1JB0 3LW5 4KT0
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit VIII, CHLOROPHYLL A, ... (16 entities in total)
Functional Keywordsphotosynthetic reaction center, membrane complex, plastocyanin, cytochrome c6, ferredoxin, electron transport
Biological sourceSynechocystis sp. PCC 6803
More
Total number of polymer chains30
Total formula weight1036491.47
Authors
Mazor, Y.,Nataf, D.,Toporik, H.,Nelson, N. (deposition date: 2013-06-13, release date: 2014-02-05, Last modification date: 2024-03-13)
Primary citationMazor, Y.,Nataf, D.,Toporik, H.,Nelson, N.
Crystal structures of virus-like photosystem I complexes from the mesophilic cyanobacterium Synechocystis PCC 6803.
Elife, 3:e01496-e01496, 2014
Cited by
PubMed Abstract: Oxygenic photosynthesis supports virtually all life forms on earth. Light energy is converted by two photosystems-photosystem I (PSI) and photosystem II (PSII). Globally, nearly 50% of photosynthesis takes place in the Ocean, where single cell cyanobacteria and algae reside together with their viruses. An operon encoding PSI was identified in cyanobacterial marine viruses. We generated a PSI that mimics the salient features of the viral complex, named PSI(PsaJF). PSI(PsaJF) is promiscuous for its electron donors and can accept electrons from respiratory cytochromes. We solved the structure of PSI(PsaJF) and a monomeric PSI, with subunit composition similar to the viral PSI, providing for the first time a detailed description of the reaction center and antenna system from mesophilic cyanobacteria, including red chlorophylls and cofactors of the electron transport chain. Our finding extends the understanding of PSI structure, function and evolution and suggests a unique function for the viral PSI. DOI: http://dx.doi.org/10.7554/eLife.01496.001.
PubMed: 24473073
DOI: 10.7554/eLife.01496
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.8 Å)
Structure validation

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数据于2025-06-18公开中

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