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- EMDB-17565: CryoEM structure of a GroEL14-GroES14 cage with two encapsulated ... -
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Open data
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Basic information
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Title | CryoEM structure of a GroEL14-GroES14 cage with two encapsulated disordered MetK substrates in the presence of ADP-BeFx | |||||||||
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![]() | Chaperonin / Folding cage / proteostasis / heat shock / ATPase / CHAPERONE | |||||||||
Function / homology | ![]() methionine adenosyltransferase / methionine adenosyltransferase activity / S-adenosylmethionine cycle / S-adenosylmethionine biosynthetic process / GroEL-GroES complex / virion assembly / potassium ion binding / chaperone cofactor-dependent protein refolding / protein folding chaperone / unfolded protein binding ...methionine adenosyltransferase / methionine adenosyltransferase activity / S-adenosylmethionine cycle / S-adenosylmethionine biosynthetic process / GroEL-GroES complex / virion assembly / potassium ion binding / chaperone cofactor-dependent protein refolding / protein folding chaperone / unfolded protein binding / protein folding / one-carbon metabolic process / protein-folding chaperone binding / response to heat / magnesium ion binding / ATP binding / identical protein binding / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.22 Å | |||||||||
![]() | Wagner J / Beck F / Bracher A / Caravajal AI / Wan W / Bohn S / Koerner R / Baumeister W / Fernandez-Busnadiego R / Hartl FU | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Visualizing chaperonin function in situ by cryo-electron tomography Authors: Wagner J / Caravajal AI / Beck F / Bracher A / Wan W / Bohn S / Koerner R / Baumeister W / Fernandez-Busnadiego R / Hartl FU | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 197.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 22.9 KB 22.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.5 KB | Display | ![]() |
Images | ![]() | 63.9 KB | ||
Masks | ![]() | 209.3 MB | ![]() | |
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 194.5 MB 194.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 21.5 KB | Display | |
Data in CIF | ![]() | 27.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8p4mC ![]() 8p4nC ![]() 8p4oC ![]() 8p4pC ![]() 8p4rC ![]() 8qxsC ![]() 8qxtC ![]() 8qxuC ![]() 8qxvC C: citing same article ( |
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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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Voxel size | X=Y=Z: 1.07 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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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_17565_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_17565_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : GroEL14-GroES14-MetK
Entire | Name: GroEL14-GroES14-MetK |
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Components |
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-Supramolecule #1: GroEL14-GroES14-MetK
Supramolecule | Name: GroEL14-GroES14-MetK / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: with bound ADP-BeF3 Mg2+ K+ |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 1.03 MDa |
-Macromolecule #1: GroEL
Macromolecule | Name: GroEL / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEITTS AWVDIEEIT RNTVREIGYV HSDMGFDANS CAVLSAIGKQ SPDINQGVDR ADPLEQGAGD Q GLMFGYAT NETDVLMPAP ITYAHRLVQR QAEVRKNGTL PWLRPDAKSQ ...String: MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEITTS AWVDIEEIT RNTVREIGYV HSDMGFDANS CAVLSAIGKQ SPDINQGVDR ADPLEQGAGD Q GLMFGYAT NETDVLMPAP ITYAHRLVQR QAEVRKNGTL PWLRPDAKSQ VTFQYDDGKI VG IDAVVLS TQHSEEIDQK SLQEAVMEEI IKPILPAEWL TSATKFFINP TGRFVIGGPM GDC GLTGRK IIVDTYGGMA RHGGGAFSGK DPSKVDRSAA YAARYVAKNI VAAGLADRCE IQVS YAIGV AEPTSIMVET FGTEKVPSEQ LTLLVREFFD LRPYGLIQML DLLHPIYKET AAYGH FGRE HFPWEKTDKA QLLRDAAGLK UniProtKB: S-adenosylmethionine synthase |
-Macromolecule #2: GroES
Macromolecule | Name: GroES / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK VGDIVIFND GYGVKSEKID NEEVLIMSES DILAIVEA UniProtKB: Co-chaperonin GroES |
-Macromolecule #3: MetK
Macromolecule | Name: MetK / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEITTS AWVDIEEIT RNTVREIGYV HSDMGFDANS CAVLSAIGKQ SPDINQGVDR ADPLEQGAGD Q GLMFGYAT NETDVLMPAP ITYAHRLVQR QAEVRKNGTL PWLRPDAKSQ ...String: MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEITTS AWVDIEEIT RNTVREIGYV HSDMGFDANS CAVLSAIGKQ SPDINQGVDR ADPLEQGAGD Q GLMFGYAT NETDVLMPAP ITYAHRLVQR QAEVRKNGTL PWLRPDAKSQ VTFQYDDGKI VG IDAVVLS TQHSEEIDQK SLQEAVMEEI IKPILPAEWL TSATKFFINP TGRFVIGGPM GDC GLTGRK IIVDTYGGMA RHGGGAFSGK DPSKVDRSAA YAARYVAKNI VAAGLADRCE IQVS YAIGV AEPTSIMVET FGTEKVPSEQ LTLLVREFFD LRPYGLIQML DLLHPIYKET AAYGH FGRE HFPWEKTDKA QLLRDAAGLK UniProtKB: S-adenosylmethionine synthase |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 10.3 mg/mL | ||||||||||||||||||||||||
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Buffer | pH: 7.4 Component:
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Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV Details: 5.9 mM n-octyl-beta-D-glucopyranoside were added before vitrification. |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 55.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 22500 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |