+Open data
-Basic information
Entry | Database: PDB / ID: 1usv | ||||||
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Title | The Structure of the complex between Aha1 and HSP90 | ||||||
Components |
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Keywords | CHAPERONE / CHAPERONE-COMPLEX / ACTIVATOR / HSP90 | ||||||
Function / homology | Function and homology information The NLRP3 inflammasome / 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 / protein targeting to mitochondrion ...The NLRP3 inflammasome / 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 / protein targeting to mitochondrion / box C/D snoRNP assembly / regulation of telomere maintenance / response to osmotic stress / 'de novo' protein folding / ATPase activator activity / protein maturation / proteasome assembly / Neutrophil degranulation / positive regulation of telomere maintenance via telomerase / ATP-dependent protein folding chaperone / protein import into nucleus / unfolded protein binding / protein folding / protein-folding chaperone binding / cellular response to heat / protein refolding / protein stabilization / perinuclear region of cytoplasm / ATP hydrolysis activity / protein-containing complex / ATP binding / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Meyer, P. / Roe, S.M. / Pearl, L.H. | ||||||
Citation | Journal: Embo J. / Year: 2004 Title: Structural Basis for Recruitment of the ATPase Activator Aha1 to the Hsp90 Chaperone Machinery. Authors: Meyer, P. / Prodromou, C. / Liao, C. / Hu, B. / Roe, S.M. / Vaughan, C.K. / Vlasic, I. / Panaretou, B. / Piper, P.W. / Pearl, L.H. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1usv.cif.gz | 320.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1usv.ent.gz | 260.4 KB | Display | PDB format |
PDBx/mmJSON format | 1usv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1usv_validation.pdf.gz | 500.2 KB | Display | wwPDB validaton report |
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Full document | 1usv_full_validation.pdf.gz | 565 KB | Display | |
Data in XML | 1usv_validation.xml.gz | 61.2 KB | Display | |
Data in CIF | 1usv_validation.cif.gz | 82.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/us/1usv ftp://data.pdbj.org/pub/pdb/validation_reports/us/1usv | HTTPS FTP |
-Related structure data
Related structure data | 1usuSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 30502.789 Da / Num. of mol.: 4 / Fragment: MIDDLE DOMAIN, RESIDUES 272-530 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P02829 #2: Protein | Mass: 19118.715 Da / Num. of mol.: 4 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1-156 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q12449 #3: Water | ChemComp-HOH / | Compound details | HSP82 IS AN ESSENTIAL PROTEIN THAT IS REQUIRED BY CELLS IN HIGH CONCENTRATIONS FOR GROWTH AT HIGHER ...HSP82 IS AN ESSENTIAL PROTEIN THAT IS REQUIRED BY CELLS IN HIGH CONCENTRAT | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 51.6 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 292 K / Method: microbatch / pH: 6.5 Details: CRYSTALS GREW FROM A MIXTURE OF MIDDLE DOMAIN HSP90 AND N- TERMINAL AHA1 AT A FINAL CONCENTRATION OF 110 UM AND 165 UM, RESPECTIVELY, IN A SOLUTION CONTAINING 90 MM AMMONIUM SULPHATE, 13.5% ...Details: CRYSTALS GREW FROM A MIXTURE OF MIDDLE DOMAIN HSP90 AND N- TERMINAL AHA1 AT A FINAL CONCENTRATION OF 110 UM AND 165 UM, RESPECTIVELY, IN A SOLUTION CONTAINING 90 MM AMMONIUM SULPHATE, 13.5% (W/V) PEG8K AND 45 MM SODIUM CACODYLATE PH 6.5 IN UNDER-OIL MICROBATCH EXPERIMENTS AT 19C. | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19 ℃ / pH: 6.5 / Method: batch method | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Nov 15, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 53437 / % possible obs: 98 % / Redundancy: 3 % / Biso Wilson estimate: 52.6 Å2 / Rmerge(I) obs: 0.104 / Net I/σ(I): 4.3 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.338 / Mean I/σ(I) obs: 2.2 / % possible all: 98 |
Reflection | *PLUS Highest resolution: 2.7 Å / Redundancy: 3 % / Rmerge(I) obs: 0.104 |
Reflection shell | *PLUS % possible obs: 94.5 % / Rmerge(I) obs: 0.338 / Mean I/σ(I) obs: 2.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1USU Resolution: 2.7→34.26 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 1501940.42 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 22.5505 Å2 / ksol: 0.273644 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 54.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.7→34.26 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.87 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 100 Å / Num. reflection obs: 53402 / Rfactor Rfree: 0.299 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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