論文

査読有り 国際誌
2021年7月1日

Cryo-EM structure of monomeric photosystem II at 2.78 Å resolution reveals factors important for the formation of dimer.

Biochimica et biophysica acta. Bioenergetics
  • Huaxin Yu
  • ,
  • Tasuku Hamaguchi
  • ,
  • Yoshiki Nakajima
  • ,
  • Koji Kato
  • ,
  • Keisuke Kawakami
  • ,
  • Fusamichi Akita
  • ,
  • Koji Yonekura
  • ,
  • Jian-Ren Shen

1862
10
開始ページ
148471
終了ページ
148471
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.bbabio.2021.148471

Photosystem II (PSII) functions mainly as a dimer to catalyze the light energy conversion and water oxidation reactions. However, monomeric PSII also exists and functions in vivo in some cases. The crystal structure of monomeric PSII has been solved at 3.6 Å resolution, but it is still not clear which factors contribute to the formation of the dimer. Here, we solved the structure of PSII monomer at a resolution of 2.78 Å using cryo-electron microscopy (cryo-EM). From our cryo-EM density map, we observed apparent differences in pigments and lipids in the monomer-monomer interface between the PSII monomer and dimer. One β-carotene and two sulfoquinovosyl diacylglycerol (SQDG) molecules are found in the monomer-monomer interface of the dimer structure but not in the present monomer structure, although some SQDG and other lipid molecules are found in the analogous region of the low-resolution crystal structure of the monomer, or cryo-EM structure of an apo-PSII monomer lacking the extrinsic proteins from Synechocystis sp. PCC 6803. In the current monomer structure, a large part of the PsbO subunit was also found to be disordered. These results indicate the importance of the β-carotene, SQDG and PsbO in formation of the PSII dimer.

リンク情報
DOI
https://doi.org/10.1016/j.bbabio.2021.148471
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/34216574
ID情報
  • DOI : 10.1016/j.bbabio.2021.148471
  • PubMed ID : 34216574

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