Summary for 9GRX
| Entry DOI | 10.2210/pdb9grx/pdb |
| EMDB information | 51527 |
| Descriptor | Photosynthetic NDH subunit of lumenal location 1, chloroplastic, Peptidyl-prolyl cis-trans isomerase, NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic, ... (55 entities in total) |
| Functional Keywords | ndh, psi, supercomplex, photosynthesis, electron transport chain, lipids, proton translocation, plastoquinone, electron transport |
| Biological source | Spinacia oleracea (spinach) More |
| Total number of polymer chains | 42 |
| Total formula weight | 1246902.51 |
| Authors | Introini, B.,Hahn, A.,Kuehlbrandt, W. (deposition date: 2024-09-13, release date: 2025-02-12, Last modification date: 2025-06-25) |
| Primary citation | Introini, B.,Hahn, A.,Kuhlbrandt, W. Cryo-EM structure of the NDH-PSI-LHCI supercomplex from Spinacia oleracea. Nat.Struct.Mol.Biol., 32:968-978, 2025 Cited by PubMed Abstract: The nicotinamide adenine dinucleotide phosphate (NADPH) dehydrogenase (NDH) complex is crucial for photosynthetic cyclic electron flow and respiration, transferring electrons from ferredoxin to plastoquinone while transporting H across the chloroplast membrane. This process boosts adenosine triphosphate production, regardless of NADPH levels. In flowering plants, NDH forms a supercomplex with photosystem I, enhancing its stability under high light. We report the cryo-electron microscopy structure of the NDH supercomplex in Spinacia oleracea at a resolution of 3.0-3.3 Å. The supercomplex consists of 41 protein subunits, 154 chlorophylls and 38 carotenoids. Subunit interactions are reinforced by 46 distinct lipids. The structure of NDH resembles that of mitochondrial complex I closely, including the quinol-binding site and an extensive internal aqueous passage for proton translocation. A well-resolved catalytic plastoquinone (PQ) occupies the PQ channel. The pronounced structural similarity to complex I sheds light on electron transfer and proton translocation within the NDH supercomplex. PubMed: 39856350DOI: 10.1038/s41594-024-01478-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.19 Å) |
Structure validation
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