7ASD

Structure of native royal jelly filaments

This is a non-PDB format compatible entry.

Summary for 7ASD

• Entry DOI: 10.2210/pdb7asd/pdb
• Related: 5YYL
• EMDB information: 11892
• Descriptor: Major royal jelly protein 1, Apisimin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: protein filament, lipoprotein, glycosylation, royal jelly, major royal jelly protein, honeybee, protein fibril
• Biological source: Apis mellifera (Honeybee); More
• Total number of polymer chains: 16
• Total formula weight: 472078.12

Authors

Mattei, S.,Ban, A.,Picenoni, A.,Leibundgut, M.,Glockshuber, R.,Boehringer, D. (deposition date: 2020-10-27, release date: 2020-12-30, Last modification date: 2024-11-13)

Primary citation

Mattei, S.,Ban, A.,Picenoni, A.,Leibundgut, M.,Glockshuber, R.,Boehringer, D.
Structure of native glycolipoprotein filaments in honeybee royal jelly.
Nat Commun, 11:6267-6267, 2020

PubMed Abstract: Royal jelly (RJ) is produced by honeybees (Apis mellifera) as nutrition during larval development. The high viscosity of RJ originates from high concentrations of long lipoprotein filaments that include the glycosylated major royal jelly protein 1 (MRJP1), the small protein apisimin and insect lipids. Using cryo-electron microscopy we reveal the architecture and the composition of RJ filaments, in which the MRJP1 forms the outer shell of the assembly, surrounding stacked apisimin tetramers harbouring tightly packed lipids in the centre. The structural data rationalize the pH-dependent disassembly of RJ filaments in the gut of the larvae.

PubMed: 33293513
DOI: 10.1038/s41467-020-20135-x

Experimental method

ELECTRON MICROSCOPY (3.5 Å)