- EMDB-33931: Structure of photosynthetic LH1-RC super-complex of Rhodobacter c... -
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Entry
Database: EMDB / ID: EMD-33931
Title
Structure of photosynthetic LH1-RC super-complex of Rhodobacter capsulatus
Map data
negative B-factor applied map
Sample
Complex: Photosynthetic LH1-RC complex from the purple phototrophic bacterium Rhodobacter capsulatus
Protein or peptide: x 6 types
Ligand: x 11 types
Function / homology
Function and homology information
organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / metal ion binding / membrane / plasma membrane Similarity search - Function
Intrinsic membrane protein family, PufX / Intrinsic membrane protein PufX / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Antenna complex, alpha/beta subunit / Light-harvesting protein B beta chain / Antenna complex, beta domain superfamily ...Intrinsic membrane protein family, PufX / Intrinsic membrane protein PufX / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Antenna complex, alpha/beta subunit / Light-harvesting protein B beta chain / Antenna complex, beta domain superfamily / Antenna complex alpha/beta subunit / Light-harvesting complex / Photosynthetic reaction centre, H subunit / Bacterial photosynthetic reaction centre, H-chain, C-terminal / Photosynthetic reaction centre, M subunit / Photosynthetic reaction centre, H subunit, N-terminal / Photosynthetic reaction centre, H subunit, N-terminal domain superfamily / Photosynthetic reaction centre, H-chain N-terminal region / PRC-barrel domain / PRC-barrel domain / Photosynthetic reaction centre, L subunit / PRC-barrel-like 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
Reaction center protein M chain / Photosynthetic reaction center H subunit / Reaction center protein L chain / Photosynthetic reaction center PufX protein / Light-harvesting protein B-870 alpha chain / Light-harvesting protein B-870 beta chain Similarity search - Component
Biological species
Rhodobacter capsulatus (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 2.6 Å
Japan Agency for Medical Research and Development (AMED)
JP21am0101118
Japan
Japan Agency for Medical Research and Development (AMED)
JP21am0101116
Japan
Japan Society for the Promotion of Science (JSPS)
JP16H04174
Japan
Japan Society for the Promotion of Science (JSPS)
JP18H05153
Japan
Japan Society for the Promotion of Science (JSPS)
20H05086
Japan
Japan Society for the Promotion of Science (JSPS)
20H02856
Japan
Citation
Journal: Nat Commun / Year: 2023 Title: Rhodobacter capsulatus forms a compact crescent-shaped LH1-RC photocomplex. Authors: Kazutoshi Tani / Ryo Kanno / Xuan-Cheng Ji / Itsusei Satoh / Yuki Kobayashi / Malgorzata Hall / Long-Jiang Yu / Yukihiro Kimura / Akira Mizoguchi / Bruno M Humbel / Michael T Madigan / Zheng-Yu Wang-Otomo / Abstract: Rhodobacter (Rba.) capsulatus has been a favored model for studies of all aspects of bacterial photosynthesis. This purple phototroph contains PufX, a polypeptide crucial for dimerization of the ...Rhodobacter (Rba.) capsulatus has been a favored model for studies of all aspects of bacterial photosynthesis. This purple phototroph contains PufX, a polypeptide crucial for dimerization of the light-harvesting 1-reaction center (LH1-RC) complex, but lacks protein-U, a U-shaped polypeptide in the LH1-RC of its close relative Rba. sphaeroides. Here we present a cryo-EM structure of the Rba. capsulatus LH1-RC purified by DEAE chromatography. The crescent-shaped LH1-RC exhibits a compact structure containing only 10 LH1 αβ-subunits. Four αβ-subunits corresponding to those adjacent to protein-U in Rba. sphaeroides were absent. PufX in Rba. capsulatus exhibits a unique conformation in its N-terminus that self-associates with amino acids in its own transmembrane domain and interacts with nearby polypeptides, preventing it from interacting with proteins in other complexes and forming dimeric structures. These features are discussed in relation to the minimal requirements for the formation of LH1-RC monomers and dimers, the spectroscopic behavior of both the LH1 and RC, and the bioenergetics of energy transfer from LH1 to the RC.
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