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Structure of the red-shifted Fittonia albivenis photosystem I.
Li, Xiuxiu; Huang, Guoqiang; Zhu, Lixia; Hao, Chenyang; Sui, Sen-Fang; Qin, Xiaochun.
Afiliación
  • Li X; School of Chemistry and Chemical Engineering, School of Biological Science and Technology, University of Jinan, Jinan, China.
  • Huang G; State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.
  • Zhu L; Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.
  • Hao C; School of Chemistry and Chemical Engineering, School of Biological Science and Technology, University of Jinan, Jinan, China.
  • Sui SF; School of Chemistry and Chemical Engineering, School of Biological Science and Technology, University of Jinan, Jinan, China.
  • Qin X; State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China. suisf@mail.tsinghua.edu.cn.
Nat Commun ; 15(1): 6325, 2024 Jul 27.
Article en En | MEDLINE | ID: mdl-39060282
ABSTRACT
Photosystem I (PSI) from Fittonia albivenis, an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI-light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microscopy. The supercomplex contains a core complex of 14 subunits and an LHCI belt with four antenna subunits (Lhca1-4) similar to previously reported angiosperm PSI-LHCI structures; however, Lhca3 differs in three regions surrounding a dimer of low-energy chlorophylls (Chls) termed red Chls, which absorb far-red beyond visible light. The unique amino acid sequences within these regions are exclusively shared by plants with strongly red-shifted fluorescence emission, suggesting candidate structural elements for regulating the energy state of red Chls. These results provide a structural basis for unraveling the mechanisms of light harvest and transfer in PSI-LHCI of under canopy plants and for designing Lhc to harness longer-wavelength light in the far-red spectral range.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Microscopía por Crioelectrón / Complejos de Proteína Captadores de Luz / Complejo de Proteína del Fotosistema I Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Microscopía por Crioelectrón / Complejos de Proteína Captadores de Luz / Complejo de Proteína del Fotosistema I Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido