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Open data
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Basic information
| Entry | ![]() | ||||||||||||||||||
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| Title | Vitellogenin from the honey bee hemolymph | ||||||||||||||||||
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Sample |
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Keywords | Yolk / LLTP / vWD / CTCK / LIPID BINDING PROTEIN | ||||||||||||||||||
| Function / homology | Function and homology informationnutrient reservoir activity / lipid transporter activity / extracellular region Similarity search - Function | ||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||||||||
Authors | Montserrat-Canals M / Schnelle K / Moeller A / Cunha E / Luecke H | ||||||||||||||||||
| Funding support | Norway, Germany, 5 items
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Citation | Journal: Nat Commun / Year: 2025Title: 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. | ||||||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_19842.map.gz | 104.9 MB | EMDB map data format | |
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| Header (meta data) | emd-19842-v30.xml emd-19842.xml | 22.4 KB 22.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_19842_fsc.xml | 10.6 KB | Display | FSC data file |
| Images | emd_19842.png | 92.7 KB | ||
| Filedesc metadata | emd-19842.cif.gz | 7.3 KB | ||
| Others | emd_19842_half_map_1.map.gz emd_19842_half_map_2.map.gz | 116.1 MB 116.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-19842 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19842 | HTTPS FTP |
-Validation report
| Summary document | emd_19842_validation.pdf.gz | 852.5 KB | Display | EMDB validaton report |
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| Full document | emd_19842_full_validation.pdf.gz | 852 KB | Display | |
| Data in XML | emd_19842_validation.xml.gz | 19 KB | Display | |
| Data in CIF | emd_19842_validation.cif.gz | 24.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19842 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19842 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9enrMC ![]() 9ensC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_19842.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.8464 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_19842_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_19842_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Vitellogenin bound to native lipids and metals
| Entire | Name: Vitellogenin bound to native lipids and metals |
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| Components |
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-Supramolecule #1: Vitellogenin bound to native lipids and metals
| Supramolecule | Name: Vitellogenin bound to native lipids and metals / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 180 KDa |
-Macromolecule #1: Vitellogenin
| Macromolecule | Name: Vitellogenin / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 201.305797 KDa |
| Sequence | String: MLLLLTLLLF AGTVAADFQH NWQVGNEYTY LVRSRTLTSL GDLSDVHTGI LIKALLTVQA KDSNVLAAKV WNGQYARVQQ SMPDGWETE ISDQMLELRD LPISGKPFQI RMKHGLIRDL IVDRDVPTWE VNILKSIVGQ LQVDTQGENA VKVNSVQVPT D DEPYASFK ...String: MLLLLTLLLF AGTVAADFQH NWQVGNEYTY LVRSRTLTSL GDLSDVHTGI LIKALLTVQA KDSNVLAAKV WNGQYARVQQ SMPDGWETE ISDQMLELRD LPISGKPFQI RMKHGLIRDL IVDRDVPTWE VNILKSIVGQ LQVDTQGENA VKVNSVQVPT D DEPYASFK AMEDSVGGKC EVLYDIAPLS DFVIHRSPEL VPMPTLKGDG RHMEVIKIKN FDNCDQRINY HFGMTDNSRL EP GTNKNGK FFSRSSTSRI VISESLKHFT IQSSVTTSKM MVSPRLYDRQ NGLVLSRMNL TLAKMEKTSK PLPMVDNPES TGN LVYIYN NPFSDVEERR VSKTAMNSNQ IVSDNSLSSS EEKLKQDILN LRTDISSSSS SISSSEENDF WQPKPTLEDA PQNS LLPNF VGYKGKHIGK SGKVDVINAA KELIFQIANE LEDASNIPVH ATLEKFMILC NLMRTMNRKQ ISELESNMQI SPNEL KPND KSQVIKQNTW TVFRDAITQT GTGPAFLTIK EWIERGTTKS MEAANIMSKL PKTVRTPTDS YIRSFFELLQ NPKVSN EQF LNTAATLSFC EMIHNAQVNK RSIHNNYPVH TFGRLTSKHD NSLYDEYIPF LERELRKAHQ EKDSPRIQTY IMALGMI GE PKILSVFEPY LEGKQQMTVF QRTLMVGSLG KLTETNPKLA RSVLYKIYLN TMESHEVRCT AVFLLMKTNP PLSMLQRM A EFTKLDTNRQ VNSAVKSTIQ SLMKLKSPEW KDLAKKARSV NHLLTHHEYD YELSRGYIDE KILENQNIIT HMILNYVGS EDSVIPRILY LTWYSSNGDI KVPSTKVLAM ISSVKSFMEL SLRSVKDRET IISAAEKIAE ELKIVPEELV PLEGNLMINN KYALKFFPF DKHILDKLPT LISNYIEAVK EGKFMNVNML DTYESVHSFP TETGLPFVYT FNVIKLTKTS GTVQAQINPD F AFIVNSNL RLTFSKNVQG RVGFVTPFEH RHFISGIDSN LHVYAPLKIS LDVNTPKGNM QWKIWPMKGE EKSRLFHYSV VP FVSNHDI LNLRPLSMEK GTRPMIPDDN TSLALPKNEG PFRLNVETAK TNEEMWELID TEKLTDRLPY PWTMDNERYV KVD MYMNLE GEQKDPVIFS TSFDSKVMTR PDTDSENWTP KMMAVEPTDK QANSKTRRQE MMREAGRGIE SAKSYVVDVR VHVP GESES ETVLTLAWSE SNVESKGRLL GFWRVEMPRS NADYEVCIGS QIMVSPETLL SYDEKMDQKP KMDFNVDIRY GKNCG KGER IDMNGKLRQS PRLKELVGAT SIIKDCVEDM KRGNKILRTC QKAVVLSMLL DEVDISMEVP SDALIALYSQ GLFSLS EID NLDVSLDVSN PKNAGKKKID VRAKLNEYLD KADVIVNTPI MDAHFKDVKL SDFGFSTEDI LDTADEDLLI NNVFYED ET SCMLDKTRAQ TFDGKDYPLR LGPCWHAVMT TYPRINPDNH NEKLHIPKDK SVSVLSRENE AGQKEVKVLL GSDKIKFV P GTTSQPEVFV NGEKIVVSRN KAYQKVEENE IIFEIYKMGD RFIGLTSDKF DVSLALDGER VMLKASEDYR YSVRGLCGN FDHDSTNDFV GPKNCLFRKP EHFVASYALI SNQCEGDSLN VAKSLQDHDC IRQERTQQRN VISDSESGRL DTEMSTWGYH HNVNKHCTI HRTQVKETDD KICFTMRPVV SCASGCTAVE TKSKPYKFHC MEKNEAAMKL KKRIEKGANP DLSQKPVSTT E ELTVPFVC KA UniProtKB: Vitellogenin |
-Macromolecule #3: [(2R)-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]o...
| Macromolecule | Name: [(2R)-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-2-propanoyloxy-propyl] propanoate type: ligand / ID: 3 / Number of copies: 1 / Formula: 43Y |
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| Molecular weight | Theoretical: 370.356 Da |
| Chemical component information | ![]() ChemComp-43Y: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1.2 mg/mL | ||||||
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| Buffer | pH: 7.6 / Component:
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 62.4 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Protocol: OTHER |
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| Output model | ![]() PDB-9enr: |
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About Yorodumi




Keywords
Authors
Norway,
Germany, 5 items
Citation




Z (Sec.)
Y (Row.)
X (Col.)





































FIELD EMISSION GUN

