- EMDB-34839: Cryo-EM structure of carotenoid-depleted RC-LH complex from Rosei... -
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Entry
Database: EMDB / ID: EMD-34839
Title
Cryo-EM structure of carotenoid-depleted RC-LH complex from Roseiflexus castenholzii at 10,000 lux
Map data
Sample
Complex: THE CAROTENOID-DEPLETED RC-LH COMPLEX
Protein or peptide: x 7 types
Ligand: x 7 types
Keywords
RC-LH core complex / PHOTOSYNTHESIS
Function / homology
Function and homology information
organelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / chlorophyll binding / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / photosynthetic electron transport in photosystem II / electron transfer activity / iron ion binding / heme binding ...organelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / chlorophyll binding / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / photosynthetic electron transport in photosystem II / electron transfer activity / iron ion binding / heme binding / membrane / metal ion binding / plasma membrane Similarity search - Function
Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta domain superfamily / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex / Antenna complex alpha/beta subunit ...Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta domain superfamily / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex / Antenna complex alpha/beta subunit / Photosynthetic reaction centre, L subunit / Multiheme cytochrome superfamily / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature. Similarity search - Domain/homology
Uncharacterized protein / Reaction center protein L chain / Alpha subunit of light-harvesting 1 / Beta subunit of light-harvesting 1 Similarity search - Component
Biological species
Roseiflexus castenholzii DSM 13941 (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 3.1 Å
National Natural Science Foundation of China (NSFC)
China
Citation
Journal: Elife / Year: 2023 Title: Carotenoid assembly regulates quinone diffusion and the reaction center-light harvesting complex architecture. Authors: Jiyu Xin / Yang Shi / Xin Zhang / Xinyi Yuan / Yueyong Xin / Huimin He / Jiejie Shen / Robert E Blankenship / Xiaoling Xu / Abstract: Carotenoid (Car) pigments perform central roles in photosynthesis-related light harvesting (LH), photoprotection, and assembly of functional pigment-protein complexes. However, the relationships ...Carotenoid (Car) pigments perform central roles in photosynthesis-related light harvesting (LH), photoprotection, and assembly of functional pigment-protein complexes. However, the relationships between Car depletion in the LH, assembly of the prokaryotic reaction center (RC)-LH complex, and quinone exchange are not fully understood. Here, we analyzed native RC-LH (nRC-LH) and Car-depleted RC-LH (dRC-LH) complexes in , a chlorosome-less filamentous anoxygenic phototroph that forms the deepest branch of photosynthetic bacteria. Newly identified exterior Cars functioned with the bacteriochlorophyll B800 to block the proposed quinone channel between LHαβ subunits in the nRC-LH, forming a sealed LH ring that was disrupted by transmembrane helices from cytochrome and subunit X to allow quinone shuttling. dRC-LH lacked subunit X, leading to an exposed LH ring with a larger opening, which together accelerated the quinone exchange rate. We also assigned amino acid sequences of subunit X and two hypothetical proteins Y and Z that functioned in forming the quinone channel and stabilizing the RC-LH interactions. This study reveals the structural basis by which Cars assembly regulates the architecture and quinone exchange of bacterial RC-LH complexes. These findings mark an important step forward in understanding the evolution and diversity of prokaryotic photosynthetic apparatus.
Name: Reaction center protein L chain / type: protein_or_peptide / ID: 3 Details: L- AND M-SUBUNITS OF THE RC ARE ENCODED BY A FUSED GENE PUFLM BUT POST-TRANSLATIONAL PROCESSED INTO TWO DISCRETE SUBUNITS EACH CONTAINING SIX AND FIVE TRANSMEMBRANE HELICES Number of copies: 1 / Enantiomer: LEVO
Name: Reaction center protein M chain / type: protein_or_peptide / ID: 4 Details: L- AND M-SUBUNITS OF THE RC ARE ENCODED BY A FUSED GENE PUFLM BUT POST-TRANSLATIONAL PROCESSED INTO TWO DISCRETE SUBUNITS EACH CONTAINING SIX AND FIVE TRANSMEMBRANE HELICES Number of copies: 1 / Enantiomer: LEVO
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