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Title | Structures of RC-LH1 complexes with open or closed quinone channels. |
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Journal, issue, pages | Sci Adv, Vol. 7, Issue 3, Year 2021 |
Publish date | Jan 13, 2021 |
![]() | David J K Swainsbury / Pu Qian / Philip J Jackson / Kaitlyn M Faries / Dariusz M Niedzwiedzki / Elizabeth C Martin / David A Farmer / Lorna A Malone / Rebecca F Thompson / Neil A Ranson / Daniel P Canniffe / Mark J Dickman / Dewey Holten / Christine Kirmaier / Andrew Hitchcock / C Neil Hunter / ![]() ![]() ![]() |
PubMed Abstract | The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo-electron microscopy structures of RC-LH1 complexes ...The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo-electron microscopy structures of RC-LH1 complexes from A 2.65-Å resolution structure of the RC-LH1-W complex consists of an open 14-subunit LH1 ring surrounding the RC interrupted by protein-W, whereas the complex without protein-W at 2.80-Å resolution comprises an RC completely encircled by a closed, 16-subunit LH1 ring. Comparison of these structures provides insights into quinone dynamics within RC-LH1 complexes, including a previously unidentified conformational change upon quinone binding at the RC Q site, and the locations of accessory quinone binding sites that aid their delivery to the RC. The structurally unique protein-W prevents LH1 ring closure, creating a channel for accelerated quinone/quinol exchange. |
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Methods | EM (single particle) |
Resolution | 2.65 - 2.8 Å |
Structure data | EMDB-11080, PDB-6z5r: EMDB-11081, PDB-6z5s: |
Chemicals | ![]() ChemComp-BCL: ![]() ChemComp-CRT: ![]() ChemComp-6PL: ![]() ChemComp-CDL: ![]() ChemComp-LMT: ![]() ChemComp-BPH: ![]() ChemComp-U10: ![]() ChemComp-FE: ![]() ChemComp-QAK: ![]() ChemComp-PGT: ![]() ChemComp-HOH: |
Source |
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![]() | PHOTOSYNTHESIS / Reaction center / Light harvesting / Protein W / Quinone |