X-ray structure of an asymmetrical trimeric ferredoxin–photosystem I complex
| Autor: | Genji Kurisu, Matthias Rögner, Risa Mutoh, Takahisa Ikegami, Pierre Sétif, Hideaki Tanaka, Kanako Shinmura, Hisako Kubota-Kawai, Marc M. Nowaczyk |
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| Přispěvatelé: | Institute for Protein Research [Osaka], Osaka University [Osaka], Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Ruhr-Universität Bochum [Bochum], Yokohama City University (YCU) |
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Magnetic Resonance Spectroscopy Protein Conformation Plant Science Protomer Crystallography X-Ray Cyanobacteria Photosystem I Chromatography Affinity Quantitative Biology::Subcellular Processes 03 medical and health sciences Electron transfer Protein structure Bacterial Proteins Binding site Ferredoxin Binding Sites Photosystem I Protein Complex Chemistry Nuclear magnetic resonance spectroscopy [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics Crystallography 030104 developmental biology Thylakoid Mutation Ferredoxins High Energy Physics::Experiment |
| Zdroj: | Nature Plants Nature Plants, 2018, 4, pp.218-224. ⟨10.1038/s41477-018-0130-0⟩ Nature Plants, Nature Publishing Group, 2018, 4, pp.218-224. ⟨10.1038/s41477-018-0130-0⟩ |
| ISSN: | 2055-0278 2055-026X |
| DOI: | 10.1038/s41477-018-0130-0 |
| Popis: | International audience; Photosystem I (PSI), a large protein complex located in the thylakoid membrane, mediates the final step in light-driven electron transfer to the stromal electron carrier protein ferredoxin (Fd). Here, we report the first structural description of the PSI–Fd complex from Thermosynechococcus elongatus. The trimeric PSI complex binds three Fds in a non-equivalent manner. While each is recognized by a PSI protomer in a similar orientation, the distances between Fds and the PSI redox centres differ. Fd binding thus entails loss of the exact three-fold symmetry of the PSI’s soluble subunits, inducing structural perturbations which are transferred to the lumen through PsaF. Affinity chromatography and nuclear magnetic resonance analyses of PSI–Fd complexes support the existence of two different Fd-binding states, with one Fd being more tightly bound than the others. We propose a dynamic structural basis for productive complex formation, which supports fast electron transfer between PSI and Fd. |
| Databáze: | OpenAIRE |
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