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Architecture of the native major royal jelly protein 1 oligomer

Author

Listed:
  • Wenli Tian

    (China Agricultural University
    Chinese Academy of Agricultural Sciences)

  • Min Li

    (China Agricultural University)

  • Huiyuan Guo

    (China Agricultural University)

  • Wenjun Peng

    (Chinese Academy of Agricultural Sciences)

  • Xiaofeng Xue

    (Chinese Academy of Agricultural Sciences)

  • Yifan Hu

    (Chinese Academy of Agricultural Sciences)

  • Yang Liu

    (China Agricultural University)

  • Yazhou Zhao

    (Chinese Academy of Agricultural Sciences)

  • Xiaoming Fang

    (Chinese Academy of Agricultural Sciences)

  • Kai Wang

    (Chinese Academy of Agricultural Sciences)

  • Xiuting Li

    (Beijing Technology and Business University)

  • Yufeng Tong

    (University of Toronto
    University of Toronto)

  • Michael A. Conlon

    (CSIRO Health and Biosecurity)

  • Wei Wu

    (China Agricultural University)

  • Fazheng Ren

    (China Agricultural University)

  • Zhongzhou Chen

    (China Agricultural University)

Abstract

Honeybee caste development is nutritionally regulated by royal jelly (RJ). Major royal jelly protein 1 (MRJP1), the most abundant glycoprotein among soluble royal jelly proteins, plays pivotal roles in honeybee nutrition and larvae development, and exhibits broad pharmacological activities in humans. However, its structure has long remained unknown. Herein, we identify and report a 16-molecule architecture of native MRJP1 oligomer containing four MRJP1, four apisimin, and eight unanticipated 24-methylenecholesterol molecules at 2.65 Å resolution. MRJP1 has a unique six-bladed β-propeller fold with three disulfide bonds, and it interacts with apisimin mainly by hydrophobic interaction. Every four 24-methylenecholesterol molecules are packaged by two MRJP1 and two apisimin molecules. This assembly dimerizes to form an H-shaped MRJP14-apisimin4-24-methylenecholesterol8 complex via apisimin in a conserved and pH-dependent fashion. Our findings offer a structural basis for understanding the pharmacological effects of MRJPs and 24-methylenecholesterol, and provide insights into their unique physiological roles in bees.

Suggested Citation

  • Wenli Tian & Min Li & Huiyuan Guo & Wenjun Peng & Xiaofeng Xue & Yifan Hu & Yang Liu & Yazhou Zhao & Xiaoming Fang & Kai Wang & Xiuting Li & Yufeng Tong & Michael A. Conlon & Wei Wu & Fazheng Ren & Zh, 2018. "Architecture of the native major royal jelly protein 1 oligomer," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05619-1
    DOI: 10.1038/s41467-018-05619-1
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