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- EMDB-16521: Cryo-EM structure of the Cibeles-Demetra 3:3 heterocomplex from G... -
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Open data
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Basic information
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Title | Cryo-EM structure of the Cibeles-Demetra 3:3 heterocomplex from Galleria mellonella saliva | ||||||||||||||||||||||||
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![]() | Galleria mellonella / Wax worm saliva / Plastic degradation / Polyethylene degradation / PEases / Hexamerin / Hemocyanin/phenoloxidase superfamily / Metal binding / Arylphorin / UNKNOWN FUNCTION | ||||||||||||||||||||||||
Function / homology | ![]() | ||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.29 Å | ||||||||||||||||||||||||
![]() | Spinola-Amilibia M / Arias-Palomo E / Araujo-Bazan L / Berger JM | ||||||||||||||||||||||||
Funding support | ![]() ![]() ![]()
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![]() | ![]() Title: Plastic degradation by insect hexamerins: Near-atomic resolution structures of the polyethylene-degrading proteins from the wax worm saliva. Authors: Mercedes Spínola-Amilibia / Ramiro Illanes-Vicioso / Elena Ruiz-López / Pere Colomer-Vidal / Francisco Rodriguez-Ventura / Rosa Peces Pérez / Clemente F Arias / Tomas Torroba / Maria ...Authors: Mercedes Spínola-Amilibia / Ramiro Illanes-Vicioso / Elena Ruiz-López / Pere Colomer-Vidal / Francisco Rodriguez-Ventura / Rosa Peces Pérez / Clemente F Arias / Tomas Torroba / Maria Solà / Ernesto Arias-Palomo / Federica Bertocchini / ![]() Abstract: Plastic waste management is a pressing ecological, social, and economic challenge. The saliva of the lepidopteran larvae is capable of oxidizing and depolymerizing polyethylene in hours at room ...Plastic waste management is a pressing ecological, social, and economic challenge. The saliva of the lepidopteran larvae is capable of oxidizing and depolymerizing polyethylene in hours at room temperature. Here, we analyze by cryo-electron microscopy (cryo-EM) 's saliva directly from the native source. The three-dimensional reconstructions reveal that the buccal secretion is mainly composed of four hexamerins belonging to the hemocyanin/phenoloxidase family, renamed Demetra, Cibeles, Ceres, and a previously unidentified factor termed Cora. Functional assays show that this factor, as its counterparts Demetra and Ceres, is also able to oxidize and degrade polyethylene. The cryo-EM data and the x-ray analysis from purified fractions show that they self-assemble primarily into three macromolecular complexes with striking structural differences that likely modulate their activity. Overall, these results establish the ground to further explore the hexamerins' functionalities, their role in vivo, and their eventual biotechnological application. | ||||||||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 187.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 24.8 KB 24.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.2 KB | Display | ![]() |
Images | ![]() | 208.8 KB | ||
Masks | ![]() | 199.6 MB | ![]() | |
Filedesc metadata | ![]() | 7.4 KB | ||
Others | ![]() ![]() ![]() | 157.8 MB 157.9 MB 157.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8ca9MC ![]() 8cadC ![]() 8canC ![]() 8po9C C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Voxel size | X=Y=Z: 0.81595 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Additional map: #1
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-Half map: #1
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-Half map: #2
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Sample components
-Entire : Cibeles-Demetra heterocomplex
Entire | Name: Cibeles-Demetra heterocomplex |
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Components |
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-Supramolecule #1: Cibeles-Demetra heterocomplex
Supramolecule | Name: Cibeles-Demetra heterocomplex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 Details: Complex of two trimeric rings of Cibeles and Demetra |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Arylphorin
Macromolecule | Name: Arylphorin / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 83.778 KDa |
Sequence | String: MQTVLFLAAL VSLAAAGYPQ YHYDVETRKL DPSLLNIQTK VLSLLENWKQ VNPDDEYYKI GKEYNVEANM ESYTNREVVT EFLSLYKAG FIPKNEVFSI FYENQALEVI ALYRLFYYAK DFETFYKTAA FARVWLNEGQ FVYAFYLAVI HRADTRGIVL P APYEIWPE ...String: MQTVLFLAAL VSLAAAGYPQ YHYDVETRKL DPSLLNIQTK VLSLLENWKQ VNPDDEYYKI GKEYNVEANM ESYTNREVVT EFLSLYKAG FIPKNEVFSI FYENQALEVI ALYRLFYYAK DFETFYKTAA FARVWLNEGQ FVYAFYLAVI HRADTRGIVL P APYEIWPE YFMNSDVLSK IYRIQMQKGL IIPEQGPYYG ILSKDNAYYF YANYSGPLTY EDNENLLSYF IEDIGWNSYY YY FHNRFPF WENGEQLIGP LKERRGEIYY YVYQKILARY YLERLANGLG EIPRFNWLDK YQTSYYPLLS SYQLPFAQRN DDY YLASGD NINDIQFIDT YEKTFLQLLQ KGQFKAYKQE VDLYNSKSIN FVGNYWQSNA DLYEKVPKRN YWRSYEATAR RVLG AAPRS SINYENMNIP TALDFYQTSL RDPAFYQLYA KILDYINEYK EYLEPYSQDV LHYVGVKIND VKVDKLVTYF EYFDW NATN AVYLSEQQLD TVSPSYIVRQ PRLNNKPFTV NIDIKSDVES EVVVKIFLGP KYDGNGLPIS LEDNWINFIE LDWFTH KLT SGQNKIARKS EEFFFFKDDS VSLFKIYELL SNGQVPSYMV DRYIYLPRRL ILPRGTQRGF PLQLFVVVYP YQAPVKE WE SMRQYIVDNK PFGYPFDRPV TLPYYFNQPN MYFKDVYVYQ EGEQYPYYNS YWSQNQVSNH UniProtKB: Arylphorin |
-Macromolecule #2: Demetra
Macromolecule | Name: Demetra / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 83.310484 KDa |
Sequence | String: MKTVLVLAAL IGLVAAGYPL FNNNVKTKTL DPNLVNIQKK VLLLLENWKQ VDPDDEYYKI GKEYNIEANI ESYTNREVVT EFLSLYKTG FTAKNQIFSI YYENQALEVR ALYRLFYYAK DFETFYKTAA FARVWLNEGQ FIYAFYIAVI HRADTRGIVL P APYEIWPE ...String: MKTVLVLAAL IGLVAAGYPL FNNNVKTKTL DPNLVNIQKK VLLLLENWKQ VDPDDEYYKI GKEYNIEANI ESYTNREVVT EFLSLYKTG FTAKNQIFSI YYENQALEVR ALYRLFYYAK DFETFYKTAA FARVWLNEGQ FIYAFYIAVI HRADTRGIVL P APYEIWPE YFVNSDVLAK INRIQMQKGL ILPETAQYYG VLAKDNAYYF YANYSGPWTY ENNENLLSYF IEDVAWNSYY YY FHSKLQF WEKGENAIGP FKERRGEIYY FIYQQILARY YLERLSNGLG EIPRFNWNDR LQAGYYPLLT THQIPFAQRN GDY YLANDD NIEDIQFVDS YEKTFLQFLQ KGQFKAYKQE VDLYNSKSVN FVGNYWQANV DLYEKVPQRN YLRSYEDAAR RILG AAPRN SYENLNVPTA LDFYQTSLRD PAFYQLYAKI LDFINQYKEY LEPYTQDVLH FVGVKINDVK VDKLVTYFEY FDWNA TNAV YLSEQQLDTG SPSYIVRQPR LNNQPFTVTI DIKSDVESEA VIKIFIGPKY DGNGYPIDLE NNWVNLVEID WFTHKL TSG QNKIERKSEN FFWFKEDSVS VSKIYELLNN GQVPRYMIEK FLLLPRRLLL PRGTEGGVPF QFFVFVYPYQ APYKEWE PM KEFVVDNKPF GYPFDRPVTE SYYFTQPNMY FKDVYIYQEG EEYPYYTSYW SQNQVPKH |
-Macromolecule #7: COPPER (II) ION
Macromolecule | Name: COPPER (II) ION / type: ligand / ID: 7 / Number of copies: 3 / Formula: CU |
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Molecular weight | Theoretical: 63.546 Da |
Chemical component information | ![]() ChemComp-CU: |
-Macromolecule #8: water
Macromolecule | Name: water / type: ligand / ID: 8 / Number of copies: 2107 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 Component:
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 2 sec. / Pretreatment - Atmosphere: AIR / Details: 25 mA | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number real images: 6386 / Average exposure time: 5.5 sec. / Average electron dose: 58.3 e/Å2 Details: Images were collected in super-resolution mode (pixel size of 0.543 angstrom) |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.6 µm / Nominal defocus min: 1.1 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL / Overall B value: 45.533 |
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Output model | ![]() PDB-8ca9: |