Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 1977, Year 2022
Publish date	Apr 13, 2022
Authors	Peng Cao / Laura Bracun / Atsushi Yamagata / Bern M Christianson / Tatsuki Negami / Baohua Zou / Tohru Terada / Daniel P Canniffe / Mikako Shirouzu / Mei Li / Lu-Ning Liu /
PubMed Abstract	The reaction center (RC) and light-harvesting complex 1 (LH1) form a RC-LH1 core supercomplex that is vital for the primary reactions of photosynthesis in purple phototrophic bacteria. Some species ...The reaction center (RC) and light-harvesting complex 1 (LH1) form a RC-LH1 core supercomplex that is vital for the primary reactions of photosynthesis in purple phototrophic bacteria. Some species possess the dimeric RC-LH1 complex with a transmembrane polypeptide PufX, representing the largest photosynthetic complex in anoxygenic phototrophs. However, the details of the architecture and assembly mechanism of the RC-LH1 dimer are unclear. Here we report seven cryo-electron microscopy (cryo-EM) structures of RC-LH1 supercomplexes from Rhodobacter sphaeroides. Our structures reveal that two PufX polypeptides are positioned in the center of the S-shaped RC-LH1 dimer, interlocking association between the components and mediating RC-LH1 dimerization. Moreover, we identify another transmembrane peptide, designated PufY, which is located between the RC and LH1 subunits near the LH1 opening. PufY binds a quinone molecule and prevents LH1 subunits from completely encircling the RC, creating a channel for quinone/quinol exchange. Genetic mutagenesis, cryo-EM structures, and computational simulations provide a mechanistic understanding of the assembly and electron transport pathways of the RC-LH1 dimer and elucidate the roles of individual components in ensuring the structural and functional integrity of the photosynthetic supercomplex.
External links	Nat Commun / PubMed:35418573 / PubMed Central
Methods	EM (single particle)
Resolution	2.74 - 4.2 Å
Structure data	31835 7va9 EMDB-31835, PDB-7va9: Rba sphaeroides PufY-KO RC-LH1 dimer type-1 Method: EM (single particle) / Resolution: 3.08 Å 31875 7vb9 EMDB-31875, PDB-7vb9: Rba sphaeroides PufY-KO RC-LH1 dimer type-2 Method: EM (single particle) / Resolution: 3.45 Å 32042 7vnm EMDB-32042, PDB-7vnm: Rba sphaeroides PufY-KO RC-LH1 monomer Method: EM (single particle) / Resolution: 2.86 Å 32047 7vny EMDB-32047, PDB-7vny: Rba sphaeroides WT RC-LH1 monomer Method: EM (single particle) / Resolution: 2.79 Å 32058 7vor EMDB-32058, PDB-7vor: The structure of dimeric photosynthetic RC-LH1 supercomplex in Class-1 Method: EM (single particle) / Resolution: 2.74 Å 32059 7vot EMDB-32059, PDB-7vot: The structure of dimeric photosynthetic RC-LH1 supercomplex in Class-2 Method: EM (single particle) / Resolution: 2.9 Å 32062 7voy EMDB-32062, PDB-7voy: Rba sphaeroides PufX-KO RC-LH1 Method: EM (single particle) / Resolution: 4.2 Å
Chemicals	ChemComp-BCL: BACTERIOCHLOROPHYLL A / Bacteriochlorophyll ChemComp-BPB: BACTERIOPHEOPHYTIN B / Pheophytin ChemComp-U10: UBIQUINONE-10 / Coenzyme Q10 ChemComp-PC1: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipidYM / Phosphatidylcholine ChemComp-FE2: Unknown entry ChemComp-SPO: SPHEROIDENE ChemComp-CDL: CARDIOLIPIN / phospholipidYM / Cardiolipin ChemComp-BPH: BACTERIOPHEOPHYTIN A / Pheophytin ChemComp-SPN: SPEROIDENONE
Source	rhodobacter sphaeroides 2.4.1 (bacteria) cereibacter sphaeroides 2.4.1 (bacteria) Cereibacter sphaeroides (bacteria)
Keywords	PHOTOSYNTHESIS / photosystem / dimer / PufY-KO / mutant / Complex / SUPERCOMPLEX / purple bacteria