8XLS

PSI-FCPI of the diatom Thalassiosira pseudonana CCMP1335

8XLS の概要

• エントリーDOI: 10.2210/pdb8xls/pdb
• EMDBエントリー: 38457
• 分子名称: Photosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XII, Photosystem I reaction center subunit Psa29, ... (32 entities in total)
• 機能のキーワード: photosystem i, electron transport, photosynthesis
• 由来する生物種: Thalassiosira pseudonana CCMP1335; 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 546618.07

構造登録者

Kato, K.,Nakajima, Y.,Shen, J.R.,Nagao, R. (登録日: 2023-12-26, 公開日: 2024-10-30, 最終更新日: 2024-11-27)

主引用文献

Kato, K.,Nakajima, Y.,Xing, J.,Kumazawa, M.,Ogawa, H.,Shen, J.R.,Ifuku, K.,Nagao, R.
Structural basis for molecular assembly of fucoxanthin chlorophyll a / c -binding proteins in a diatom photosystem I supercomplex.
Elife, 13:-, 2024

PubMed Abstract: Photosynthetic organisms exhibit remarkable diversity in their light-harvesting complexes (LHCs). LHCs are associated with photosystem I (PSI), forming a PSI-LHCI supercomplex. The number of LHCI subunits, along with their protein sequences and pigment compositions, has been found to differ greatly among the PSI-LHCI structures. However, the mechanisms by which LHCIs recognize their specific binding sites within the PSI core remain unclear. In this study, we determined the cryo-electron microscopy structure of a PSI supercomplex incorporating fucoxanthin chlorophyll /-binding proteins (FCPs), designated as PSI-FCPI, isolated from the diatom CCMP1335. Structural analysis of PSI-FCPI revealed five FCPI subunits associated with a PSI monomer; these subunits were identified as RedCAP, Lhcr3, Lhcq10, Lhcf10, and Lhcq8. Through structural and sequence analyses, we identified specific protein-protein interactions at the interfaces between FCPI and PSI subunits, as well as among FCPI subunits themselves. Comparative structural analyses of PSI-FCPI supercomplexes, combined with phylogenetic analysis of FCPs from and the diatom , underscore the evolutionary conservation of protein motifs crucial for the selective binding of individual FCPI subunits. These findings provide significant insights into the molecular mechanisms underlying the assembly and selective binding of FCPIs in diatoms.

PubMed: 39480899
DOI: 10.7554/eLife.99858

実験手法

ELECTRON MICROSCOPY (2.3 Å)