7RF4

RT XFEL structure of Photosystem II 50 microseconds after the second illumination at 2.27 Angstrom resolution

This is a non-PDB format compatible entry.

Summary for 7RF4

• Entry DOI: 10.2210/pdb7rf4/pdb
• Descriptor: Photosystem II protein D1 1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (37 entities in total)
• Functional Keywords: photosynthesis, membrane protein, photosystem ii
• Biological source: Thermosynechococcus elongatus (strain BP-1); More
• Total number of polymer chains: 40
• Total formula weight: 758362.30

Authors

Hussein, R.,Ibrahim, M.,Bhowmick, A.,Simon, P.S.,Chatterjee, R.,Lassalle, L.,Doyle, M.D.,Bogacz, I.,Kim, I.-S.,Cheah, M.H.,Gul, S.,de Lichtenberg, C.,Chernev, P.,Pham, C.C.,Young, I.D.,Carbajo, S.,Fuller, F.D.,Alonso-Mori, R.,Batyuk, A.,Sutherlin, K.D.,Brewster, A.S.,Bolotovski, R.,Mendez, D.,Holton, J.M.,Moriarty, N.W.,Adams, P.D.,Bergmann, U.,Sauter, N.K.,Dobbek, H.,Messinger, J.,Zouni, A.,Kern, J.,Yachandra, V.K.,Yano, J. (deposition date: 2021-07-13, release date: 2021-11-10, Last modification date: 2023-10-18)

Primary citation

Hussein, R.,Ibrahim, M.,Bhowmick, A.,Simon, P.S.,Chatterjee, R.,Lassalle, L.,Doyle, M.,Bogacz, I.,Kim, I.S.,Cheah, M.H.,Gul, S.,de Lichtenberg, C.,Chernev, P.,Pham, C.C.,Young, I.D.,Carbajo, S.,Fuller, F.D.,Alonso-Mori, R.,Batyuk, A.,Sutherlin, K.D.,Brewster, A.S.,Bolotovsky, R.,Mendez, D.,Holton, J.M.,Moriarty, N.W.,Adams, P.D.,Bergmann, U.,Sauter, N.K.,Dobbek, H.,Messinger, J.,Zouni, A.,Kern, J.,Yachandra, V.K.,Yano, J.
Structural dynamics in the water and proton channels of photosystem II during the S 2 to S 3 transition.
Nat Commun, 12:6531-6531, 2021

PubMed Abstract: Light-driven oxidation of water to molecular oxygen is catalyzed by the oxygen-evolving complex (OEC) in Photosystem II (PS II). This multi-electron, multi-proton catalysis requires the transport of two water molecules to and four protons from the OEC. A high-resolution 1.89 Å structure obtained by averaging all the S states and refining the data of various time points during the S to S transition has provided better visualization of the potential pathways for substrate water insertion and proton release. Our results indicate that the O1 channel is the likely water intake pathway, and the Cl1 channel is the likely proton release pathway based on the structural rearrangements of water molecules and amino acid side chains along these channels. In particular in the Cl1 channel, we suggest that residue D1-E65 serves as a gate for proton transport by minimizing the back reaction. The results show that the water oxidation reaction at the OEC is well coordinated with the amino acid side chains and the H-bonding network over the entire length of the channels, which is essential in shuttling substrate waters and protons.

PubMed: 34764256
DOI: 10.1038/s41467-021-26781-z

Experimental method

X-RAY DIFFRACTION (2.27 Å)