6A7K
X-ray structure of NdhS from T. elongatus
Summary for 6A7K
| Entry DOI | 10.2210/pdb6a7k/pdb |
| Descriptor | Tlr0636 protein, ACETIC ACID (3 entities in total) |
| Functional Keywords | nadh dehydrogenase-like complex, ndh-1, cyclic electron flow (cef), ferredoxin, electron transport |
| Biological source | Thermosynechococcus elongatus (strain BP-1) |
| Total number of polymer chains | 2 |
| Total formula weight | 16567.22 |
| Authors | Umeno, K.,Misumi, Y.,Tanaka, H.,Kurisu, G. (deposition date: 2018-07-03, release date: 2019-01-16, Last modification date: 2023-11-22) |
| Primary citation | Schuller, J.M.,Birrell, J.A.,Tanaka, H.,Konuma, T.,Wulfhorst, H.,Cox, N.,Schuller, S.K.,Thiemann, J.,Lubitz, W.,Setif, P.,Ikegami, T.,Engel, B.D.,Kurisu, G.,Nowaczyk, M.M. Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. Science, 363:257-260, 2019 Cited by PubMed Abstract: Photosynthetic complex I enables cyclic electron flow around photosystem I, a regulatory mechanism for photosynthetic energy conversion. We report a 3.3-angstrom-resolution cryo-electron microscopy structure of photosynthetic complex I from the cyanobacterium The model reveals structural adaptations that facilitate binding and electron transfer from the photosynthetic electron carrier ferredoxin. By mimicking cyclic electron flow with isolated components in vitro, we demonstrate that ferredoxin directly mediates electron transfer between photosystem I and complex I, instead of using intermediates such as NADPH (the reduced form of nicotinamide adenine dinucleotide phosphate). A large rate constant for association of ferredoxin to complex I indicates efficient recognition, with the protein subunit NdhS being the key component in this process. PubMed: 30573545DOI: 10.1126/science.aau3613 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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