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Structure paper

TitleStructural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 1977, Year 2022
Publish dateApr 13, 2022
AuthorsPeng 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 AbstractThe 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 linksNat Commun / PubMed:35418573 / PubMed Central
MethodsEM (single particle)
Resolution2.74 - 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

ChemComp-BPB:
BACTERIOPHEOPHYTIN B

ChemComp-U10:
UBIQUINONE-10

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-FE2:
Unknown entry

ChemComp-SPO:
SPHEROIDENE

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-BPH:
BACTERIOPHEOPHYTIN A

ChemComp-SPN:
SPEROIDENONE

Source
  • rhodobacter sphaeroides 2.4.1 (bacteria)
  • cereibacter sphaeroides 2.4.1 (bacteria)
KeywordsPHOTOSYNTHESIS / photosystem / dimer / PufY-KO / mutant / Complex / SUPERCOMPLEX / purple bacteria

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