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Open data
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Basic information
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Title | High resolution map of molecular chaperone Artemin | |||||||||
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Function / homology | ![]() ferroxidase / ferroxidase activity / ferric iron binding / iron ion transport / intracellular iron ion homeostasis Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.04 Å | |||||||||
![]() | Parvate AD / Powell SM / Brookreason JT / Novikova IV / Evans JE | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of the diapause chaperone artemin. Authors: Amar D Parvate / Samantha M Powell / Jory T Brookreson / Trevor H Moser / Irina V Novikova / Mowei Zhou / James E Evans / ![]() Abstract: The protein artemin acts as both an RNA and protein chaperone and constitutes over 10% of all protein in cysts during diapause. However, its mechanistic details remain elusive since no high- ...The protein artemin acts as both an RNA and protein chaperone and constitutes over 10% of all protein in cysts during diapause. However, its mechanistic details remain elusive since no high-resolution structure of artemin exists. Here we report the full-length structure of artemin at 2.04 Å resolution. The cryo-EM map contains density for an intramolecular disulfide bond between Cys22-Cys61 and resolves the entire C-terminus extending into the core of the assembled protein cage but in a different configuration than previously hypothesized with molecular modeling. We also provide data supporting the role of C-terminal helix F towards stabilizing the dimer form that is believed to be important for its chaperoning activity. We were able to destabilize this effect by placing a tag at the C-terminus to fully pack the internal cavity and cause limited steric hindrance. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 436.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 11.5 KB 11.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 25.2 KB | Display | ![]() |
Images | ![]() | 46.6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 529.5 KB | Display | ![]() |
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Full document | ![]() | 529 KB | Display | |
Data in XML | ![]() | 19.5 KB | Display | |
Data in CIF | ![]() | 27.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7rvbMC 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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Related items in Molecule of the Month |
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Map
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Annotation | Unsharpened map | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.3398 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : 24mer Artemin complex
Entire | Name: 24mer Artemin complex |
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Components |
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-Supramolecule #1: 24mer Artemin complex
Supramolecule | Name: 24mer Artemin complex / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 624 MDa |
-Macromolecule #1: Ferritin
Macromolecule | Name: Ferritin / type: protein_or_peptide / ID: 1 / Number of copies: 24 / Enantiomer: LEVO / EC number: ferroxidase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 26.144912 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MATEGARNIG QSAPEGKVQM DCPSRHNFDP ECEKAFVEHI HLELASSYHA WSMWAFYARD CKAAVGMTRL CEWASHVSAQ RARRMAAYV LTRGGHVDYK EIPAPKKQGW DNFEDAFSHC VANKKRILTS LQSLYQCCQS KDAHCSNFIQ TDMMDEVIAW N KFLSDCLS ...String: MATEGARNIG QSAPEGKVQM DCPSRHNFDP ECEKAFVEHI HLELASSYHA WSMWAFYARD CKAAVGMTRL CEWASHVSAQ RARRMAAYV LTRGGHVDYK EIPAPKKQGW DNFEDAFSHC VANKKRILTS LQSLYQCCQS KDAHCSNFIQ TDMMDEVIAW N KFLSDCLS NLHCIGSQGM GPWVFDRWLA RIVMSKFKHP KIPSLSTSDL ESNIPNELFD AEGDMVRAIK KL |
-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 |
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 2595 / Average exposure time: 1.5 sec. / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Protocol: AB INITIO MODEL |
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Output model | ![]() PDB-7rvb: |