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- EMDB-22242: Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-22242 | ||||||||||||||||||
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Title | Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP | ||||||||||||||||||
![]() | Hsc82 in complex with Aha1 in the presence of AMP-PNP | ||||||||||||||||||
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Function / homology | ![]() Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / Extra-nuclear estrogen signaling / VEGFR2 mediated vascular permeability / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / HSF1-dependent transactivation / HSF1 activation / response to oxygen levels / box C/D snoRNP assembly / ATPase activator activity ...Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / Extra-nuclear estrogen signaling / VEGFR2 mediated vascular permeability / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / HSF1-dependent transactivation / 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 / disordered domain specific binding / 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 / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||
Biological species | ![]() ![]() | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.15 Å | ||||||||||||||||||
![]() | Liu YX / Sun M / Myasnikov AG / Elnatan D / Agard DA | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() 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 |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.1 KB 13.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.1 KB | Display | ![]() |
Images | ![]() | 79.3 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 550 KB | Display | ![]() |
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Full document | ![]() | 549.6 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 14.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6xlfMC ![]() 6xlbC ![]() 6xlcC ![]() 6xldC ![]() 6xleC ![]() 6xlgC ![]() 6xlhC 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
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Hsc82 in complex with Aha1 in the presence of AMP-PNP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.059 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 : Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP
Entire | Name: Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP |
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Components |
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-Supramolecule #1: Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP
Supramolecule | Name: Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() ![]() Strain: ATCC 204508 / S288c |
Recombinant expression | Organism: ![]() ![]() |
-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: ![]() ![]() Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 81.003594 KDa |
Recombinant expression | Organism: ![]() ![]() |
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 |
-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: ![]() ![]() Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 39.486422 KDa |
Recombinant expression | Organism: ![]() ![]() |
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 |
-Macromolecule #3: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Macromolecule | Name: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / type: ligand / ID: 3 / Number of copies: 2 / Formula: ANP |
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Molecular weight | Theoretical: 506.196 Da |
Chemical component information | ![]() ChemComp-ANP: |
-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 |
-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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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 72.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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Output model | ![]() PDB-6xlf: |