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7RF8

RT XFEL structure of the two-flash state of Photosystem II (2F, S3-rich) at 2.09 Angstrom resolution

This is a non-PDB format compatible entry.
Summary for 7RF8
Entry DOI10.2210/pdb7rf8/pdb
DescriptorPhotosystem II protein D1 1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (37 entities in total)
Functional Keywordsphotosynthesis, membrane protein, photosystem ii
Biological sourceThermosynechococcus elongatus (strain BP-1)
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Total number of polymer chains40
Total formula weight758862.36
Authors
Primary citationHussein, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.09 Å)
Structure validation

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