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Title | Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution. |
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Journal, issue, pages | Sci Adv, Vol. 7, Issue 25, Year 2021 |
Publish date | Jun 16, 2021 |
Authors | Laura Bracun / Atsushi Yamagata / Bern M Christianson / Tohru Terada / Daniel P Canniffe / Mikako Shirouzu / Lu-Ning Liu / |
PubMed 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. |
External links | Sci Adv / PubMed:34134992 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.84 Å |
Structure data | EMDB-30656, PDB-7ddq: |
Chemicals | ChemComp-BCL: ChemComp-SPO: ChemComp-U10: ChemComp-BPH: ChemComp-FE: ChemComp-3PE: |
Source |
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Keywords | PHOTOSYNTHESIS / membrane protein / light-harvesting / reaction center / pufx |