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5YYL

Structure of Major Royal Jelly Protein 1 Oligomer

Summary for 5YYL
Entry DOI10.2210/pdb5yyl/pdb
DescriptorMajor royal jelly protein 1, Apisimin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordscomplex, royal jelly, signaling protein
Biological sourceApis mellifera (Honeybee)
More
Total number of polymer chains4
Total formula weight116008.71
Authors
Tian, W.,Chen, Z. (deposition date: 2017-12-10, release date: 2018-08-08, Last modification date: 2024-10-30)
Primary citationTian, W.,Li, M.,Guo, H.,Peng, W.,Xue, X.,Hu, Y.,Liu, Y.,Zhao, Y.,Fang, X.,Wang, K.,Li, X.,Tong, Y.,Conlon, M.A.,Wu, W.,Ren, F.,Chen, Z.
Architecture of the native major royal jelly protein 1 oligomer.
Nat Commun, 9:3373-3373, 2018
Cited by
PubMed 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 MRJP1-apisimin-24-methylenecholesterol 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.
PubMed: 30135511
DOI: 10.1038/s41467-018-05619-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

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