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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-5248 | |||||||||
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Title | Mm-cpn rls deltalid with ATP and AlFx | |||||||||
![]() | This is the density map of Mm-cpn rls deltalid mutant in the ATP and AlFx state. | |||||||||
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![]() | Mm-cpn / maripaludis / chaperonin | |||||||||
Function / homology | ![]() chaperonin-containing T-complex / ATP-dependent protein folding chaperone / unfolded protein binding / ATP hydrolysis activity / ATP binding / identical protein binding / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.2 Å | |||||||||
![]() | Douglas NR / Reissmann S / Zhang J / Chen B / Jakana J / Kumar R / Chiu W / Frydman J | |||||||||
![]() | ![]() Title: Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber. Authors: Nicholai R Douglas / Stefanie Reissmann / Junjie Zhang / Bo Chen / Joanita Jakana / Ramya Kumar / Wah Chiu / Judith Frydman / ![]() Abstract: Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins ...Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins within the central chaperonin chamber. Here, we describe the fate of the substrate during the nucleotide cycle of group II chaperonins. The chaperonin substrate-binding sites are exposed, and the lid is open in both the ATP-free and ATP-bound prehydrolysis states. ATP hydrolysis has a dual function in the folding cycle, triggering both lid closure and substrate release into the central chamber. Notably, substrate release can occur in the absence of a lid, and lid closure can occur without substrate release. However, productive folding requires both events, so that the polypeptide is released into the confined space of the closed chamber where it folds. Our results show that ATP hydrolysis coordinates the structural and functional determinants that trigger productive folding. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 28.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 8.2 KB 8.2 KB | Display Display | ![]() |
Images | ![]() | 150.5 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3izlMC ![]() 5244C ![]() 5245C ![]() 5246C ![]() 5247C ![]() 5249C ![]() 5250C ![]() 3izhC ![]() 3iziC ![]() 3izjC ![]() 3izkC ![]() 3izmC ![]() 3iznC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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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 | This is the density map of Mm-cpn rls deltalid mutant in the ATP and AlFx state. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.33 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Mm-cpn rls deltalid with ATP and AlFx
Entire | Name: Mm-cpn rls deltalid with ATP and AlFx |
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Components |
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-Supramolecule #1000: Mm-cpn rls deltalid with ATP and AlFx
Supramolecule | Name: Mm-cpn rls deltalid with ATP and AlFx / type: sample / ID: 1000 / Oligomeric state: 16-mer / Number unique components: 1 |
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Molecular weight | Experimental: 900 KDa / Theoretical: 900 KDa |
-Macromolecule #1: chaperonin
Macromolecule | Name: chaperonin / type: protein_or_peptide / ID: 1 / Name.synonym: Mm-cpn / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() |
Molecular weight | Experimental: 900 KDa / Theoretical: 900 KDa |
Recombinant expression | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: OTHER / Details: Vitrification instrument: vitrobot |
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Electron microscopy
Microscope | JEOL 3200FSC |
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Image recording | Category: FILM / Film or detector model: GENERIC GATAN (4k x 4k) / Digitization - Scanner: OTHER |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Sample stage | Specimen holder: Gatan side entry / Specimen holder model: GATAN LIQUID NITROGEN |
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Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.2 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: EMAN |
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