5ZF0

X-ray Structure of the Electron Transfer Complex between Ferredoxin and Photosystem I

This is a non-PDB format compatible entry.

Summary for 5ZF0

• Entry DOI: 10.2210/pdb5zf0/pdb
• Descriptor: Photosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XI, Photosystem I reaction center subunit XII, ... (21 entities in total)
• Functional Keywords: photosystem i, ferredoxin, photosynthesis-electron transport complex, photosynthesis/electron transport
• Biological source: Thermosynechococcus elongatus BP-1; More
• Cellular location: Cellular thylakoid membrane ; Multi- pass membrane protein : P0A405 Q8DGB4 P0A407 P0A425; Cellular thylakoid membrane ; Single-pass membrane protein : P0A403 P0A427 P0A429; Cellular thylakoid membrane ; Peripheral membrane protein ; Cytoplasmic side : P0A415; Cellular thylakoid membrane ; Peripheral membrane protein : P0A423
• Total number of polymer chains: 78
• Total formula weight: 2223592.25

Authors

Kubota-Kawai, H.,Mutoh, R.,Shinmura, K.,Setif, P.,Nowaczyk, M.,Roegner, M.,Ikegami, T.,Tanaka, T.,Kurisu, G. (deposition date: 2018-03-01, release date: 2018-04-11, Last modification date: 2024-10-23)

Primary citation

Kubota-Kawai, H.,Mutoh, R.,Shinmura, K.,Setif, P.,Nowaczyk, M.M.,Rogner, M.,Ikegami, T.,Tanaka, H.,Kurisu, G.
X-ray structure of an asymmetrical trimeric ferredoxin-photosystem I complex
Nat Plants, 4:218-224, 2018

PubMed Abstract: 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.

PubMed: 29610537
DOI: 10.1038/s41477-018-0130-0

Experimental method

X-RAY DIFFRACTION (4.2 Å)