叶绿体
光系统I
普通大麦
低温电子层析成像
蛋白质亚单位
NADH脱氢酶
电子传输链
生物
生物物理学
类囊体
光合作用
光系统II
化学
生物化学
植物
物理
基因
禾本科
光学
断层摄影术
作者
Liangliang Shen,Kailu Tang,Wenda Wang,Chen Wang,Hangjun Wu,Zhiyuan Mao,Shaoya An,Shenghai Chang,Tingyun Kuang,Jian‐Ren Shen,Guangye Han,Xing Zhang
出处
期刊:Nature
[Springer Nature]
日期:2021-12-08
卷期号:601 (7894): 649-654
被引量:42
标识
DOI:10.1038/s41586-021-04277-6
摘要
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.
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