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- PDB-9ens: Cleavage product of vitellogenin from the honey bee hemolymph -

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Basic information

Entry
Database: PDB / ID: 9ens
TitleCleavage product of vitellogenin from the honey bee hemolymph
ComponentsVitellogenin
KeywordsLIPID BINDING PROTEIN / Yolk / LLTP / zinc / vitellogenesis
Function / homology
Function and homology information


nutrient reservoir activity / lipid transporter activity / extracellular region
Similarity search - Function
: / Vitellinogen, open beta-sheet / Vitellinogen, open beta-sheet / DUF1943 / Vitellogenin, N-terminal / Lipovitellin-phosvitin complex, superhelical domain / Vitellinogen, beta-sheet N-terminal / Lipid transport protein, beta-sheet shell / Lipoprotein amino terminal region / Vitellogenin domain profile. ...: / Vitellinogen, open beta-sheet / Vitellinogen, open beta-sheet / DUF1943 / Vitellogenin, N-terminal / Lipovitellin-phosvitin complex, superhelical domain / Vitellinogen, beta-sheet N-terminal / Lipid transport protein, beta-sheet shell / Lipoprotein amino terminal region / Vitellogenin domain profile. / Lipoprotein N-terminal Domain / von Willebrand factor, type D domain / von Willebrand factor type D domain / VWFD domain profile. / von Willebrand factor (vWF) type D domain
Similarity search - Domain/homology
Biological speciesApis cerana (Asiatic honeybee)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å
AuthorsMontserrat-Canals, M. / Schnelle, K. / Moeller, A. / Cunha, E. / Luecke, H.
Funding support Norway, Germany, 5items
OrganizationGrant numberCountry
Norwegian Research Council262137 Norway
Norwegian Research Council335244 Norway
German Research Foundation (DFG)SFB 944 Germany
German Research Foundation (DFG)SFB 1557 Germany
German Research Foundation (DFG)INST190/196-1 FUGG Germany
CitationJournal: Nat Commun / Year: 2025
Title: Cryo-EM structure of native honey bee vitellogenin.
Authors: Mateu Montserrat-Canals / Kilian Schnelle / Vilde Leipart / Øyvind Halskau / Gro V Amdam / Arne Moeller / Eva S Cunha / Hartmut Luecke /
Abstract: 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 ...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.
History
DepositionMar 13, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 26, 2025Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Vitellogenin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)202,2172
Polymers201,3061
Non-polymers9111
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1210 Å2
ΔGint16 kcal/mol
Surface area54560 Å2
MethodPISA

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Components

#1: Protein Vitellogenin


Mass: 201305.797 Da / Num. of mol.: 1
Fragment: The cleavage site for this sample is unclear as there are four possible cleavage sites at positions 1276, 1283, 1318 and 1321; hence the full-length protein sequence is listed.
Source method: isolated from a natural source
Details: The cleavage site for this sample is unclear as there are four possible cleavage sites at positions 1276, 1283, 1318 and 1321; hence the full-length protein sequence is listed.
Source: (natural) Apis cerana (Asiatic honeybee) / References: UniProt: Q868N5
#2: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Vitellogenin bound to native lipids and metals / Type: COMPLEX / Entity ID: #1 / Source: NATURAL
Molecular weightValue: 0.15 MDa / Experimental value: YES
Source (natural)Organism: Apis cerana (Asiatic honeybee) / Tissue: Hemolymph
Buffer solutionpH: 7.6
Buffer component
IDConc.NameBuffer-ID
10.5 MTris-HCl1
20.2 MNaCl1
SpecimenConc.: 1.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 298 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2800 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 62.4 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.1particle selection
4cryoSPARC4.1CTF correction
9PHENIXmodel refinement
10cryoSPARC4.2initial Euler assignment
11cryoSPARC4.2final Euler assignment
13cryoSPARC4.23D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1180000 / Symmetry type: POINT
Atomic model buildingProtocol: OTHER
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0049266
ELECTRON MICROSCOPYf_angle_d0.56612572
ELECTRON MICROSCOPYf_dihedral_angle_d5.1421280
ELECTRON MICROSCOPYf_chiral_restr0.0451450
ELECTRON MICROSCOPYf_plane_restr0.0041609

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