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Yorodumi- EMDB-22244: Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound w... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-22244 | ||||||||||||||||||
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Title | Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS | ||||||||||||||||||
Map data | Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS | ||||||||||||||||||
Sample |
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Keywords | Co-chaperone / activator / CHAPERONE | ||||||||||||||||||
Function / homology | Function and homology information ESR-mediated signaling / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / Extra-nuclear estrogen signaling / VEGFR2 mediated vascular permeability / HSF1-dependent transactivation / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / HSF1 activation / response to oxygen levels / : ...ESR-mediated signaling / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / Extra-nuclear estrogen signaling / VEGFR2 mediated vascular permeability / HSF1-dependent transactivation / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / HSF1 activation / response to oxygen levels / : / box C/D snoRNP assembly / ATPase activator activity / proteasome assembly / Neutrophil degranulation / telomere maintenance / ATP-dependent protein folding chaperone / unfolded protein binding / protein folding / cellular response to heat / protein-folding chaperone binding / protein stabilization / perinuclear region of cytoplasm / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.83 Å | ||||||||||||||||||
Authors | Liu YX / Sun M | ||||||||||||||||||
Funding support | United States, 5 items
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Citation | Journal: To Be Published Title: Cryo-EM structures reveal a multistep mechanism of Hsp90 activation by co-chaperone Aha1 Authors: Liu YX / Sun M / Myasnikov AG / Elnatan D / Agard DA | ||||||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_22244.map.gz | 117 MB | EMDB map data format | |
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Header (meta data) | emd-22244-v30.xml emd-22244.xml | 13.3 KB 13.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_22244_fsc.xml | 11.4 KB | Display | FSC data file |
Images | emd_22244.png | 68.4 KB | ||
Filedesc metadata | emd-22244.cif.gz | 6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-22244 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-22244 | HTTPS FTP |
-Related structure data
Related structure data | 6xlhMC 6xlbC 6xlcC 6xldC 6xleC 6xlfC 6xlgC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_22244.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.822 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound w...
Entire | Name: Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS |
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Components |
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-Supramolecule #1: Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound w...
Supramolecule | Name: Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c |
-Macromolecule #1: ATP-dependent molecular chaperone HSC82
Macromolecule | Name: ATP-dependent molecular chaperone HSC82 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 81.003594 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL SDPKQLETEP DLFIRITPKP EEKVLEIRDS GIGMTKAEL INNLGTIAKS GTKAFMEALS AGADVSMIGQ FGVGFYSLFL VADRVQVISK NNEDEQYIWE SNAGGSFTVT L DEVNERIG ...String: MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL SDPKQLETEP DLFIRITPKP EEKVLEIRDS GIGMTKAEL INNLGTIAKS GTKAFMEALS AGADVSMIGQ FGVGFYSLFL VADRVQVISK NNEDEQYIWE SNAGGSFTVT L DEVNERIG RGTVLRLFLK DDQLEYLEEK RIKEVIKRHS EFVAYPIQLL VTKEVEKEVP IPEEEKKDEE KKDEDDKKPK LE EVDEEEE EKKPKTKKVK EEVQELEELN KTKPLWTRNP SDITQEEYNA FYKSISNDWE DPLYVKHFSV EGQLEFRAIL FIP KRAPFD LFESKKKKNN IKLYVRRVFI TDEAEDLIPE WLSFVKGVVD SEDLPLNLSR EMLQQNKIMK VIRKNIVKKL IEAF NEIAE DSEQFDKFYS AFAKNIKLGV HEDTQNRAAL AKLLRYNSTK SVDELTSLTD YVTRMPEHQK NIYYITGESL KAVEK SPFL DALKAKNFEV LFLTDPIDEY AFTQLKEFEG KTLVDITKDF ELEETDEEKA EREKEIKEYE PLTKALKDIL GDQVEK VVV SYKLLDAPAA IRTGQFGWSA NMERIMKAQA LRDSSMSSYM SSKKTFEISP KSPIIKELKK RVDEGGAQDK TVKDLTN LL FETALLTSGF SLEEPTSFAS RINRLISLGL NIDEDEETET APEASTEAPV EEVPADTEME EVD UniProtKB: ATP-dependent molecular chaperone HSC82 |
-Macromolecule #2: Hsp90 co-chaperone AHA1
Macromolecule | Name: Hsp90 co-chaperone AHA1 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 39.486422 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MVVNNPNNWH WVDKNCIGWA KEYFKQKLVG VEAGSVKDKK YAKIKSVSSI EGDCEVNQRK GKVISLFDLK ITVLIEGHVD SKDGSALPF EGSINVPEVA FDSEASSYQF DISIFKETSE LSEAKPLIRS ELLPKLRQIF QQFGKDLLAT HGNDIQVPES Q VKSNYTRG ...String: MVVNNPNNWH WVDKNCIGWA KEYFKQKLVG VEAGSVKDKK YAKIKSVSSI EGDCEVNQRK GKVISLFDLK ITVLIEGHVD SKDGSALPF EGSINVPEVA FDSEASSYQF DISIFKETSE LSEAKPLIRS ELLPKLRQIF QQFGKDLLAT HGNDIQVPES Q VKSNYTRG NQKSSFTEIK DSASKPKKNA LPSSTSTSAP VSSTNKVPQN GSGNSTSIYL EPTFNVPSSE LYETFLDKQR IL AWTRSAQ FFNSGPKLET KEKFELFGGN VISELVSCEK DKKLVFHWKL KDWSAPFNST IEMTFHESQE FHETKLQVKW TGI PVGEED RVRANFEEYY VRSIKLTFGF GAVL UniProtKB: Hsp90 co-chaperone AHA1 |
-Macromolecule #3: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
Macromolecule | Name: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / type: ligand / ID: 3 / Number of copies: 1 / Formula: AGS |
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Molecular weight | Theoretical: 523.247 Da |
Chemical component information | ChemComp-AGS: |
-Macromolecule #4: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #5: POTASSIUM ION
Macromolecule | Name: POTASSIUM ION / type: ligand / ID: 5 / Number of copies: 2 / Formula: K |
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Molecular weight | Theoretical: 39.098 Da |
-Macromolecule #6: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 6 / Number of copies: 1 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ChemComp-ADP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 72.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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Output model | PDB-6xlh: |