Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution.
Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution.
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光合作用RC-LH1-PufX超配合物在2.8-Å分辨率下的低温电镜结构
DOI:
10.1126/sciadv.abf8864
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发表时间:
2021-06
期刊:
影响因子:
13.6
通讯作者:
Liu LN
中科院分区:
文献类型:
--
作者:
Bracun L;Yamagata A;Christianson BM;Terada T;Canniffe DP;Shirouzu M;Liu LN
Atomic structure of the first RC-LH1-PufX supercomplex provides new insights into the assembly and function of photosynthetic systems. 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 Rhodobacter veldkampii 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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DOI:
10.1073/pnas.162368399
发表时间:
2002-08-20
影响因子:
11.1
作者:
Camara-Artigas, A;Brune, D;Allen, JP
通讯作者:
Allen, JP
影响因子:
5.5
作者:
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通讯作者:
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影响因子:
3.3
作者:
Klauda, Jeffery B.;Venable, Richard M.;Freites, J. Alfredo;O'Connor, Joseph W.;Tobias, Douglas J.;Mondragon-Ramirez, Carlos;Vorobyov, Igor;MacKerell, Alexander D., Jr.;Pastor, Richard W.
通讯作者:
Pastor, Richard W.
影响因子:
5.5
作者:
Hess, Berk
通讯作者:
Hess, Berk
影响因子:
5.5
作者:
Best, Robert B.;Zhu, Xiao;Shim, Jihyun;Lopes, Pedro E. M.;Mittal, Jeetain;Feig, Michael;MacKerell, Alexander D., Jr.
通讯作者:
MacKerell, Alexander D., Jr.