- EMDB-30656: Structure of RC-LH1-PufX from Rhodobacter veldkampii -
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Basic information
Entry
Database: EMDB / ID: EMD-30656
Title
Structure of RC-LH1-PufX from Rhodobacter veldkampii
Map data
Sample
Complex: Photosynthetic core complex featuring reaction center, LH1 and PufX
Protein or peptide: x 4 types
Protein or peptide: x 2 types
Ligand: x 6 types
Keywords
membrane protein / light-harvesting / reaction center / pufx / PHOTOSYNTHESIS
Function / homology
Function and homology information
organelle inner membrane / : / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / photosynthetic electron transport in photosystem II / membrane => GO:0016020 / metal ion binding / 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. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex ...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. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex / Antenna complex alpha/beta subunit / 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
Antenna pigment protein beta chain / Reaction center protein M chain / Uncharacterized protein / Photosynthetic reaction center subunit H / Antenna pigment protein alpha chain / Photosynthetic reaction center L subunit Similarity search - Component
Biological species
Rhodobacter veldkampii DSM 11550 (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 2.84 Å
Biotechnology and Biological Sciences Research Council (BBSRC)
R003890
United Kingdom
Japan Agency for Medical Research and Development (AMED)
JP20am0101082
Japan
Japan Agency for Medical Research and Development (AMED)
JP20am0101115
Japan
Japan Society for the Promotion of Science (JSPS)
JP 19H03162
Japan
Citation
Journal: Sci Adv / Year: 2021 Title: Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution. Authors: Laura Bracun / Atsushi Yamagata / Bern M Christianson / Tohru Terada / Daniel P Canniffe / Mikako Shirouzu / Lu-Ning Liu / Abstract: The reaction center (RC)-light-harvesting complex 1 (LH1) supercomplex plays a pivotal role in bacterial photosynthesis. Many RC-LH1 complexes integrate an additional protein PufX that is key for ...The reaction center (RC)-light-harvesting complex 1 (LH1) supercomplex plays a pivotal role in bacterial photosynthesis. Many RC-LH1 complexes integrate an additional protein PufX that is key for bacterial growth and photosynthetic competence. Here, we present a cryo-electron microscopy structure of the RC-LH1-PufX supercomplex from at 2.8-Å resolution. The RC-LH1-PufX monomer contains an LH ring of 15 αβ-polypeptides with a 30-Å gap formed by PufX. PufX acts as a molecular "cross brace" to reinforce the RC-LH1 structure. The unusual PufX-mediated large opening in the LH1 ring and defined arrangement of proteins and cofactors provide the molecular basis for the assembly of a robust RC-LH1-PufX supercomplex and efficient quinone transport and electron transfer. These architectural features represent the natural strategies for anoxygenic photosynthesis and environmental adaptation.
History
Deposition
Oct 29, 2020
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Header (metadata) release
Jun 30, 2021
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Map release
Jun 30, 2021
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Update
Mar 27, 2024
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Current status
Mar 27, 2024
Processing site: PDBj / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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