6L7P

cryo-EM structure of cyanobacteria NDH-1LdelV complex

Summary for 6L7P

• Entry DOI: 10.2210/pdb6l7p/pdb
• EMDB information: 0849 0850
• Descriptor: NAD(P)H-quinone oxidoreductase subunit 1, NAD(P)H-quinone oxidoreductase subunit J, NAD(P)H-quinone oxidoreductase subunit K, ... (25 entities in total)
• Functional Keywords: photosystem i, cyclic electron transfer, photosynthesis
• Biological source: Thermosynechococcus elongatus BP-1; More
• Total number of polymer chains: 18
• Total formula weight: 522859.02

Authors

Zhang, C.,Shuai, J.,Wu, J.,Lei, M. (deposition date: 2019-11-02, release date: 2020-02-19, Last modification date: 2024-05-29)

Primary citation

Zhang, C.,Shuai, J.,Ran, Z.,Zhao, J.,Wu, Z.,Liao, R.,Wu, J.,Ma, W.,Lei, M.
Structural insights into NDH-1 mediated cyclic electron transfer.
Nat Commun, 11:888-888, 2020

PubMed Abstract: NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis. Here, we report a 3.2-Å-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from the cyanobacterium Thermosynechococcus elongatus. The structure reveals three β-carotene and fifteen lipid molecules in the membrane arm of NDH-1L. Regulatory oxygenic photosynthesis-specific (OPS) subunits NdhV, NdhS and NdhO are close to the Fd-binding site whilst NdhL is adjacent to the plastoquinone (PQ) cavity, and they play different roles in PSI CET under high-light stress. NdhV assists in the binding of Fd to NDH-1L and accelerates PSI CET in response to short-term high-light exposure. In contrast, prolonged high-light irradiation switches on the expression and assembly of the NDH-1MS complex, which likely contains no NdhO to further accelerate PSI CET and reduce ROS production. We propose that this hierarchical mechanism is necessary for the survival of cyanobacteria in an aerobic environment.

PubMed: 32060291
DOI: 10.1038/s41467-020-14732-z

Experimental method

ELECTRON MICROSCOPY (3.6 Å)