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8YGL

Rhodobacter blasticus RC-LH1 monomer

Summary for 8YGL
Entry DOI10.2210/pdb8ygl/pdb
EMDB information39255
DescriptorAntenna pigment protein beta chain, CARDIOLIPIN, BACTERIOPHEOPHYTIN A, ... (13 entities in total)
Functional Keywordsphotosynthesis, light-harvesting complex
Biological sourceFuscovulum blasticum DSM 2131
More
Total number of polymer chains34
Total formula weight361517.51
Authors
Liu, L.N.,Zhang, Y.Z.,Wang, P.,Christianson, B.M.,Ugurlar, D. (deposition date: 2024-02-26, release date: 2025-03-05)
Primary citationWang, P.,Christianson, B.M.,Ugurlar, D.,Mao, R.,Zhang, Y.,Liu, Z.K.,Zhang, Y.Y.,Gardner, A.M.,Gao, J.,Zhang, Y.Z.,Liu, L.N.
Architectures of photosynthetic RC-LH1 supercomplexes from Rhodobacter blasticus.
Sci Adv, 10:eadp6678-eadp6678, 2024
Cited by
PubMed Abstract: The reaction center-light-harvesting complex 1 (RC-LH1) plays an essential role in the primary reactions of bacterial photosynthesis. Here, we present high-resolution structures of native monomeric and dimeric RC-LH1 supercomplexes from () using cryo-electron microscopy. The RC-LH1 monomer is composed of an RC encircled by an open LH1 ring comprising 15 αβ heterodimers and a PufX transmembrane polypeptide. In the RC-LH1 dimer, two crossing PufX polypeptides mediate dimerization. Unlike counterpart, RC-LH1 dimer has a less bent conformation, lacks the PufY subunit near the LH1 opening, and includes two extra LH1 αβ subunits, forming a more enclosed S-shaped LH1 ring. Spectroscopic assays reveal that these unique structural features are accompanied by changes in the kinetics of quinone/quinol trafficking between RC-LH1 and cytochrome . Our findings reveal the assembly principles and structural variability of photosynthetic RC-LH1 supercomplexes, highlighting diverse strategies used by phototrophic bacteria to optimize light-harvesting and electron transfer in competitive environments.
PubMed: 39383221
DOI: 10.1126/sciadv.adp6678
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.6 Å)
Structure validation

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