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7Z6Q

Cryo-EM structure of the whole photosynthetic complex from the green sulfur bacteria

Summary for 7Z6Q
Entry DOI10.2210/pdb7z6q/pdb
EMDB information14528
DescriptorPhotosystem P840 reaction center, large subunit, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE, [(2~{R})-2-hexadecanoyloxy-3-[(2~{S},3~{S},4~{R},5~{R},6~{S})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-propyl] hexadecanoate, ... (14 entities in total)
Functional Keywordsreaction centre, electron transport, energy transfer, green sulfur bacterium, membrane protein, light-harvesting protein complex, photosynthesis
Biological sourceChlorobaculum tepidum TLS
More
Total number of polymer chains12
Total formula weight569591.81
Authors
Xie, H.,Tsiotis, G. (deposition date: 2022-03-14, release date: 2023-02-08, Last modification date: 2025-10-01)
Primary citationXie, H.,Lyratzakis, A.,Khera, R.,Koutantou, M.,Welsch, S.,Michel, H.,Tsiotis, G.
Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacterium Chlorobaculum tepidum.
Proc.Natl.Acad.Sci.USA, 120:e2216734120-e2216734120, 2023
Cited by
PubMed Abstract: Light energy absorption and transfer are very important processes in photosynthesis. In green sulfur bacteria light is absorbed primarily by the chlorosomes and its energy is transferred via the Fenna-Matthews-Olson (FMO) proteins to a homodimeric reaction center (RC). Here, we report the cryogenic electron microscopic structure of the intact FMO-RC apparatus from at 2.5 Å resolution. The FMO-RC apparatus presents an asymmetric architecture and contains two FMO trimers that show different interaction patterns with the RC core. Furthermore, the two permanently bound transmembrane subunits PscC, which donate electrons to the special pair, interact only with the two large PscA subunits. This structure fills an important gap in our understanding of the transfer of energy from antenna to the electron transport chain of this RC and the transfer of electrons from reduced sulfur compounds to the special pair.
PubMed: 36693097
DOI: 10.1073/pnas.2216734120
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.5 Å)
Structure validation

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