7RF5

RT XFEL structure of Photosystem II 150 microseconds after the second illumination at 2.23 Angstrom resolution

これはPDB形式変換不可エントリーです。

7RF5 の概要

• エントリーDOI: 10.2210/pdb7rf5/pdb
• 分子名称: Photosystem II protein D1 1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (37 entities in total)
• 機能のキーワード: photosynthesis, membrane protein
• 由来する生物種: Thermosynechococcus elongatus (strain BP-1); 詳細
• タンパク質・核酸の鎖数: 40
• 化学式量合計: 759050.97

構造登録者

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. (登録日: 2021-07-13, 公開日: 2021-11-10, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.23 Å)