6KHI
Supercomplex for cylic electron transport in cyanobacteria
Summary for 6KHI
Entry DOI | 10.2210/pdb6khi/pdb |
EMDB information | 9989 9990 |
Descriptor | NAD(P)H-quinone oxidoreductase subunit 1, NAD(P)H-quinone oxidoreductase subunit J, NAD(P)H-quinone oxidoreductase subunit K, ... (27 entities in total) |
Functional Keywords | cylic electron transport, photosynthetic ndh complex, cyanobacteria, electron transport |
Biological source | Thermosynechococcus elongatus BP-1 More |
Total number of polymer chains | 20 |
Total formula weight | 493452.31 |
Authors | |
Primary citation | Pan, X.,Cao, D.,Xie, F.,Xu, F.,Su, X.,Mi, H.,Zhang, X.,Li, M. Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase. Nat Commun, 11:610-610, 2020 Cited by PubMed Abstract: NAD(P)H dehydrogenase-like (NDH) complex NDH-1L of cyanobacteria plays a crucial role in cyclic electron flow (CEF) around photosystem I and respiration processes. NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen that drives the ATP production. NDH-1L-dependent CEF increases the ATP/NADPH ratio, and is therefore pivotal for oxygenic phototrophs to function under stress. Here we report two structures of NDH-1L from Thermosynechococcus elongatus BP-1, in complex with one Fd and an endogenous PQ, respectively. Our structures represent the complete model of cyanobacterial NDH-1L, revealing the binding manner of NDH-1L with Fd and PQ, as well as the structural elements crucial for proper functioning of the NDH-1L complex. Together, our data provides deep insights into the electron transport from Fd to PQ, and its coupling with proton translocation in NDH-1L. PubMed: 32001694DOI: 10.1038/s41467-020-14456-0 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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