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-Structure paper
タイトル | Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution. |
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ジャーナル・号・ページ | Sci Adv, Vol. 7, Issue 25, Year 2021 |
掲載日 | 2021年6月16日 |
![]() | Laura Bracun / Atsushi Yamagata / Bern M Christianson / Tohru Terada / Daniel P Canniffe / Mikako Shirouzu / Lu-Ning Liu / ![]() ![]() ![]() |
PubMed 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 2.84 Å |
構造データ | EMDB-30656, PDB-7ddq: |
化合物 | ![]() ChemComp-BCL: ![]() ChemComp-SPO: ![]() ChemComp-BPH: ![]() ChemComp-FE: ![]() ChemComp-3PE: |
由来 |
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![]() | PHOTOSYNTHESIS / membrane protein / light-harvesting / reaction center / pufx |