Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP

• Kawakami, Tomoaki

• Yu, Long-Jiang

• Liang, Tai

• Okazaki, Koudai

• Madigan, Michael T.

• 木村, 行宏

• Wang-Otomo, Zheng-Yu

抄録

Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling. HiPIP binds to the surface of the tetraheme cytochrome subunit in the light-harvesting (LH1) complex-associated RC in close proximity to the low-potential heme-1 group. The binding interface between the two proteins is primarily formed by uncharged residues and is characterized by hydrophobic features. This co-crystal structure provides a model for the detailed study of long-range trans-protein electron tunneling pathways in biological systems.

収録刊行物

• Nature Communications

  Nature Communications 12 (1), 1104-1104, 2021-02-17

  Nature Research

キーワード

• General Physics and Astronomy
• General Biochemistry, Genetics and Molecular Biology
• General Chemistry
• Multidisciplinary

詳細情報

• CRID: 1050856995322008192
• NII論文ID: 120006996935
• NII書誌ID: AA12645905
• DOI: 10.1038/s41467-021-21397-9
• ISSN: 20411723
• HANDLE: 20.500.14094/90007992
• Web Site: https://www.nature.com/articles/s41467-021-21397-9.pdf
• Web Site: https://www.nature.com/articles/s41467-021-21397-9
• 本文言語コード: en
• 資料種別: journal article
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