|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 & Zhongzhou Chen. Architecture of the native major royal jelly protein 1|
Architecture of the native major royal jelly protein 1 oligome
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 & Zhongzhou Chen
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 2.65Å 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.