| Literature DB >> 34879391 |
Liangliang Shen1,2, Kailu Tang3, Wenda Wang1, Chen Wang3, Hangjun Wu4, Zhiyuan Mao1,2, Shaoya An3,4, Shenghai Chang4, Tingyun Kuang1, Jian-Ren Shen5,6, Guangye Han7, Xing Zhang8,9,10.
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.Entities:
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Year: 2021 PMID： 34879391 DOI： 10.1038/s41586-021-04277-6
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 69.504