Architecture of the chloroplast PSI–NDH supercomplex in Hordeum vulgare

Liangliang Shen, Kailu Tang, Wenda Wang, Chen Wang, Hangjun Wu, Zhiyuan Mao, Shaoya An, Shenghai Chang, Tingyun Kuang, Jian-Ren Shen (), Guangye Han () and Xing Zhang ()
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Liangliang Shen: Chinese Academy of Sciences
Kailu Tang: Zhejiang University School of Medicine
Wenda Wang: Chinese Academy of Sciences
Chen Wang: Zhejiang University School of Medicine
Hangjun Wu: Zhejiang University School of Medicine
Zhiyuan Mao: Chinese Academy of Sciences
Shaoya An: Zhejiang University School of Medicine
Shenghai Chang: Zhejiang University School of Medicine
Tingyun Kuang: Chinese Academy of Sciences
Jian-Ren Shen: Chinese Academy of Sciences
Guangye Han: Chinese Academy of Sciences
Xing Zhang: Zhejiang University School of Medicine

Nature, 2022, vol. 601, issue 7894, 649-654

Abstract: Abstract The chloroplast NADH dehydrogenase-like (NDH) complex is composed of at least 29 subunits and has an important role in mediating photosystem I (PSI) cyclic electron transport (CET)1–3. The NDH complex associates with PSI to form the PSI–NDH supercomplex and fulfil its function. Here, we report cryo-electron microscopy structures of a PSI–NDH supercomplex from barley (Hordeum vulgare). The structures reveal that PSI–NDH is composed of two copies of the PSI–light-harvesting complex I (LHCI) subcomplex and one NDH complex. Two monomeric LHCI proteins, Lhca5 and Lhca6, mediate the binding of two PSI complexes to NDH. Ten plant chloroplast-specific NDH subunits are presented and their exact positions as well as their interactions with other subunits in NDH are elucidated. In all, this study provides a structural basis for further investigations on the functions and regulation of PSI–NDH-dependent CET.

Date: 2022
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DOI: 10.1038/s41586-021-04277-6

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