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, Xing Zhang

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)649-654
Number of pages6
JournalNature
Volume601
Issue number7894
DOIs
Publication statusPublished - Jan 27 2022

ASJC Scopus subject areas

  • General

Fingerprint

Dive into the research topics of 'Architecture of the chloroplast PSI–NDH supercomplex in Hordeum vulgare'. Together they form a unique fingerprint.

Cite this