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光合反应中心-LH1-PufX超复合物的2.8埃分辨率冷冻电镜结构。

Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution.

作者信息

Bracun Laura, Yamagata Atsushi, Christianson Bern M, Terada Tohru, Canniffe Daniel P, Shirouzu Mikako, Liu Lu-Ning

机构信息

Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK.

Laboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.

出版信息

Sci Adv. 2021 Jun 16;7(25). doi: 10.1126/sciadv.abf8864. Print 2021 Jun.

DOI:10.1126/sciadv.abf8864
PMID:34134992
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8208714/
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 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.

摘要

反应中心（RC）-光捕获复合物1（LH1）超复合物在细菌光合作用中起关键作用。许多RC-LH1复合物整合了一种额外的蛋白质PufX，它对细菌生长和光合能力至关重要。在此，我们展示了来自[具体来源未给出]的RC-LH1-PufX超复合物在2.8埃分辨率下的冷冻电子显微镜结构。RC-LH1-PufX单体包含一个由15个αβ多肽组成的LH环，PufX形成了一个30埃的间隙。PufX作为分子“交叉支撑”来加强RC-LH1结构。LH1环中由PufX介导的异常大开口以及蛋白质和辅因子的特定排列为稳健的RC-LH1-PufX超复合物的组装以及高效的醌转运和电子转移提供了分子基础。这些结构特征代表了无氧光合作用和环境适应的自然策略。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/eb121316b9ab/abf8864-F5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/cb526589db05/abf8864-F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/8a5867aac4ce/abf8864-F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/f1410cfaca7a/abf8864-F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/ec8ad3333fdc/abf8864-F4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/eb121316b9ab/abf8864-F5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/cb526589db05/abf8864-F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/8a5867aac4ce/abf8864-F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/f1410cfaca7a/abf8864-F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/ec8ad3333fdc/abf8864-F4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1fc1/8208714/eb121316b9ab/abf8864-F5.jpg

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