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Cryo-EM structure of native honey bee vitellogenin
by
Montserrat-Canals, Mateu
, Moeller, Arne
, Leipart, Vilde
, Schnelle, Kilian
, Halskau, Øyvind
, Amdam, Gro V.
, Cunha, Eva S.
, Luecke, Hartmut
in
101/28
/ 631/337/458/1524
/ 631/45/612/1191
/ 631/535/1258/1259
/ 631/601/1466
/ Amino Acid Sequence
/ Animals
/ Apis mellifera
/ Bees
/ Bees - metabolism
/ Binding
/ Chemical bonds
/ Cryoelectron Microscopy
/ Crystal structure
/ Egg laying
/ Eggs
/ Hemolymph
/ Hemolymph - metabolism
/ Homology
/ Honey
/ Humanities and Social Sciences
/ Insect Proteins - chemistry
/ Insect Proteins - metabolism
/ Insect Proteins - ultrastructure
/ Lipids
/ Models, Molecular
/ Molecular modelling
/ multidisciplinary
/ Post-translation
/ Protein Domains
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Silver
/ Social behavior
/ Social organization
/ Structural members
/ Structure-function relationships
/ Vitellogenin
/ Vitellogenins - chemistry
/ Vitellogenins - genetics
/ Vitellogenins - isolation & purification
/ Vitellogenins - metabolism
/ Vitellogenins - ultrastructure
/ Von Willebrand factor
2025
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Cryo-EM structure of native honey bee vitellogenin
by
Montserrat-Canals, Mateu
, Moeller, Arne
, Leipart, Vilde
, Schnelle, Kilian
, Halskau, Øyvind
, Amdam, Gro V.
, Cunha, Eva S.
, Luecke, Hartmut
in
101/28
/ 631/337/458/1524
/ 631/45/612/1191
/ 631/535/1258/1259
/ 631/601/1466
/ Amino Acid Sequence
/ Animals
/ Apis mellifera
/ Bees
/ Bees - metabolism
/ Binding
/ Chemical bonds
/ Cryoelectron Microscopy
/ Crystal structure
/ Egg laying
/ Eggs
/ Hemolymph
/ Hemolymph - metabolism
/ Homology
/ Honey
/ Humanities and Social Sciences
/ Insect Proteins - chemistry
/ Insect Proteins - metabolism
/ Insect Proteins - ultrastructure
/ Lipids
/ Models, Molecular
/ Molecular modelling
/ multidisciplinary
/ Post-translation
/ Protein Domains
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Silver
/ Social behavior
/ Social organization
/ Structural members
/ Structure-function relationships
/ Vitellogenin
/ Vitellogenins - chemistry
/ Vitellogenins - genetics
/ Vitellogenins - isolation & purification
/ Vitellogenins - metabolism
/ Vitellogenins - ultrastructure
/ Von Willebrand factor
2025
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Cryo-EM structure of native honey bee vitellogenin
by
Montserrat-Canals, Mateu
, Moeller, Arne
, Leipart, Vilde
, Schnelle, Kilian
, Halskau, Øyvind
, Amdam, Gro V.
, Cunha, Eva S.
, Luecke, Hartmut
in
101/28
/ 631/337/458/1524
/ 631/45/612/1191
/ 631/535/1258/1259
/ 631/601/1466
/ Amino Acid Sequence
/ Animals
/ Apis mellifera
/ Bees
/ Bees - metabolism
/ Binding
/ Chemical bonds
/ Cryoelectron Microscopy
/ Crystal structure
/ Egg laying
/ Eggs
/ Hemolymph
/ Hemolymph - metabolism
/ Homology
/ Honey
/ Humanities and Social Sciences
/ Insect Proteins - chemistry
/ Insect Proteins - metabolism
/ Insect Proteins - ultrastructure
/ Lipids
/ Models, Molecular
/ Molecular modelling
/ multidisciplinary
/ Post-translation
/ Protein Domains
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Silver
/ Social behavior
/ Social organization
/ Structural members
/ Structure-function relationships
/ Vitellogenin
/ Vitellogenins - chemistry
/ Vitellogenins - genetics
/ Vitellogenins - isolation & purification
/ Vitellogenins - metabolism
/ Vitellogenins - ultrastructure
/ Von Willebrand factor
2025
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Journal Article
Cryo-EM structure of native honey bee vitellogenin
2025
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Overview
Vitellogenin (Vg) is the main yolk precursor lipoprotein in almost all egg-laying animals. In addition, along its evolutionary history, Vg has developed a range of new functions in different taxa. In the honey bee, Vg has functions related to immunity, antioxidant protection, social behavior and longevity. However, the molecular mechanisms underlying Vg functionalities are still poorly understood. Here, we report the cryo-EM structure of full-length honey bee Vg, one-step purified directly from hemolymph. The structure provides structural insights into the overall domain architecture, including the lipid binding cavity and the previously uncharacterized von Willebrand factor type D domain. A domain of unknown function has been identified as a C-terminal cystine knot domain based on structural homology. Information about post-translational modifications, cleavage products, metal and lipid binding allow an improved understanding of the mechanisms underlying the range of Vg functionalities. The findings have numerous implications for the structure-function relationship of vitellogenins of other species as well as members of the same protein superfamily, which share the same structural elements.
Vitellogenin is present in almost all egg-laying animals and is known for its multiple functions in reproduction, immunity and social organization. Here, the authors present the cryo-EM structure of native Vitellogenin from the honey bee.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Animals
/ Bees
/ Binding
/ Eggs
/ Homology
/ Honey
/ Humanities and Social Sciences
/ Insect Proteins - metabolism
/ Insect Proteins - ultrastructure
/ Lipids
/ Proteins
/ Science
/ Silver
/ Structure-function relationships
/ Vitellogenins - isolation & purification
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