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- EMDB-23050: Atomic cryoEM structure of Hsp90-Hsp70-Hop-GR -

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Entry
Database: EMDB / ID: EMD-23050
TitleAtomic cryoEM structure of Hsp90-Hsp70-Hop-GR
Map dataRaw (unsharpened) map from Relion's refine3d.
Sample
  • Complex: Hsp90-Hsp70-Hop-GR complex
    • Complex: Heat shock protein HSP 90-alphaHeat shock response
      • Protein or peptide: Heat shock protein HSP 90-alphaHeat shock response
    • Complex: Heat shock 70 kDa protein 1A
      • Protein or peptide: Heat shock 70 kDa protein 1A
    • Complex: Stress-induced-phosphoprotein 1
      • Protein or peptide: Stress-induced-phosphoprotein 1
    • Complex: Glucocorticoid receptor
      • Protein or peptide: Glucocorticoid receptor
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: POTASSIUM IONPotassium
KeywordsClient-loading / CHAPERONE
Function / homology
Function and homology information


positive regulation of endoribonuclease activity / denatured protein binding / Regulation of NPAS4 gene transcription / cellular heat acclimation / regulation of glucocorticoid biosynthetic process / nuclear glucocorticoid receptor activity / death receptor agonist activity / negative regulation of inclusion body assembly / Viral RNP Complexes in the Host Cell Nucleus / positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway ...positive regulation of endoribonuclease activity / denatured protein binding / Regulation of NPAS4 gene transcription / cellular heat acclimation / regulation of glucocorticoid biosynthetic process / nuclear glucocorticoid receptor activity / death receptor agonist activity / negative regulation of inclusion body assembly / Viral RNP Complexes in the Host Cell Nucleus / positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / C3HC4-type RING finger domain binding / dynein axonemal particle / steroid hormone binding / PTK6 Expression / ATP-dependent protein disaggregase activity / positive regulation of microtubule nucleation / neuroinflammatory response / glucocorticoid metabolic process / microglia differentiation / mammary gland duct morphogenesis / misfolded protein binding / maternal behavior / regulation of mitotic spindle assembly / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / positive regulation of tumor necrosis factor-mediated signaling pathway / astrocyte differentiation / cellular response to interleukin-7 / protein folding chaperone complex / transcription regulator inhibitor activity / cellular response to glucocorticoid stimulus / aggresome / RND1 GTPase cycle / motor behavior / lysosomal transport / sperm mitochondrial sheath / dATP binding / Scavenging by Class F Receptors / sulfonylurea receptor binding / CTP binding / positive regulation of protein polymerization / vRNP Assembly / UTP binding / sperm plasma membrane / positive regulation of tau-protein kinase activity / protein insertion into mitochondrial outer membrane / regulation of gluconeogenesis / chaperone-mediated autophagy / telomerase holoenzyme complex assembly / adrenal gland development / Rho GDP-dissociation inhibitor binding / cellular response to steroid hormone stimulus / Uptake and function of diphtheria toxin / mitochondrial transport / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib / Resistance of ERBB2 KD mutants to neratinib / Resistance of ERBB2 KD mutants to osimertinib / Resistance of ERBB2 KD mutants to afatinib / Resistance of ERBB2 KD mutants to AEE788 / Resistance of ERBB2 KD mutants to lapatinib / Drug resistance in ERBB2 TMD/JMD mutants / PIWI-interacting RNA (piRNA) biogenesis / TPR domain binding / non-chaperonin molecular chaperone ATPase / regulation of postsynaptic membrane neurotransmitter receptor levels / mRNA catabolic process / dendritic growth cone / chaperone cofactor-dependent protein refolding / Sema3A PAK dependent Axon repulsion / regulation of protein ubiquitination / skeletal muscle contraction / positive regulation of cell size / HSF1-dependent transactivation / telomere maintenance via telomerase / response to unfolded protein / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / chaperone-mediated protein complex assembly / Regulation of HSF1-mediated heat shock response / protein unfolding / HSF1 activation / regulation of protein-containing complex assembly / Attenuation phase / cellular response to unfolded protein / estrogen response element binding / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / RHOBTB2 GTPase cycle / positive regulation of lamellipodium assembly / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / eNOS activation / axonal growth cone / DNA polymerase binding / intracellular steroid hormone receptor signaling pathway / ATP metabolic process / core promoter sequence-specific DNA binding / protein folding chaperone / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / inclusion body / Loss of Nlp from mitotic centrosomes
Similarity search - Function
STI1/HOP, DP domain / STI1/HOP, DP domain / Tetratricopeptide repeat 2 / Tetratricopeptide repeat / Glucocorticoid receptor / Glucocorticoid receptor / Heat shock chaperonin-binding / Heat shock chaperonin-binding motif. / TPR repeat / Tetratricopeptide repeat ...STI1/HOP, DP domain / STI1/HOP, DP domain / Tetratricopeptide repeat 2 / Tetratricopeptide repeat / Glucocorticoid receptor / Glucocorticoid receptor / Heat shock chaperonin-binding / Heat shock chaperonin-binding motif. / TPR repeat / Tetratricopeptide repeat / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. / Heat shock protein 70, conserved site / Heat shock protein 70kD, peptide-binding domain superfamily / Heat shock protein 70 family / Hsp70 protein / Heat shock protein 70kD, C-terminal domain superfamily / Tetratricopeptide repeat / Heat shock protein Hsp90, conserved site / Heat shock hsp90 proteins family signature. / HSP90, C-terminal domain / Heat shock protein Hsp90, N-terminal / Heat shock protein Hsp90 family / Hsp90 protein / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / ATPase, nucleotide binding domain / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily / Ligand-binding domain of nuclear hormone receptor / Nuclear receptor (NR) ligand-binding (LBD) domain profile. / Ligand binding domain of hormone receptors / Zinc finger, NHR/GATA-type / Tetratricopeptide-like helical domain superfamily / Ribosomal protein S5 domain 2-type fold
Similarity search - Domain/homology
Glucocorticoid receptor / Heat shock protein HSP 90-alpha / Heat shock 70 kDa protein 1A / Stress-induced-phosphoprotein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.57 Å
AuthorsWang RY / Noddings CM
Funding support United States, 1 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Nature / Year: 2022
Title: Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism.
Authors: Ray Yu-Ruei Wang / Chari M Noddings / Elaine Kirschke / Alexander G Myasnikov / Jill L Johnson / David A Agard /
Abstract: Maintaining a healthy proteome is fundamental for the survival of all organisms. Integral to this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding, remodelling and ...Maintaining a healthy proteome is fundamental for the survival of all organisms. Integral to this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding, remodelling and maturation of the many 'client proteins' of Hsp90. The glucocorticoid receptor (GR) is a model client protein that is strictly dependent on Hsp90 and Hsp70 for activity. Chaperoning GR involves a cycle of inactivation by Hsp70; formation of an inactive GR-Hsp90-Hsp70-Hop 'loading' complex; conversion to an active GR-Hsp90-p23 'maturation' complex; and subsequent GR release. However, to our knowledge, a molecular understanding of this intricate chaperone cycle is lacking for any client protein. Here we report the cryo-electron microscopy structure of the GR-loading complex, in which Hsp70 loads GR onto Hsp90, uncovering the molecular basis of direct coordination by Hsp90 and Hsp70. The structure reveals two Hsp70 proteins, one of which delivers GR and the other scaffolds the Hop cochaperone. Hop interacts with all components of the complex, including GR, and poises Hsp90 for subsequent ATP hydrolysis. GR is partially unfolded and recognized through an extended binding pocket composed of Hsp90, Hsp70 and Hop, revealing the mechanism of GR loading and inactivation. Together with the GR-maturation complex structure, we present a complete molecular mechanism of chaperone-dependent client remodelling, and establish general principles of client recognition, inhibition, transfer and activation.
History
DepositionNov 30, 2020-
Header (metadata) releaseDec 8, 2021-
Map releaseDec 8, 2021-
UpdateMay 29, 2024-
Current statusMay 29, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.011
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  • Surface view with fitted model
  • Atomic models: PDB-7kw7
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_23050.png

Downloads & links

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Map

FileDownload / File: emd_23050.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationRaw (unsharpened) map from Relion's refine3d.
Voxel sizeX=Y=Z: 1.059 Å
Density
Contour LevelBy EMDB: 0.008 / Movie #1: 0.011
Minimum - Maximum-0.019397546 - 0.06302023
Average (Standard dev.)-0.00011620503 (±0.0020187232)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 338.88 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0591.0591.059
M x/y/z320320320
origin x/y/z0.0000.0000.000
length x/y/z338.880338.880338.880
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS320320320
D min/max/mean-0.0190.063-0.000

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Supplemental data

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Half map: Unfiltered half1 map from Relion's refine3d.

Fileemd_23050_half_map_1.map
AnnotationUnfiltered half1 map from Relion's refine3d.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Unfiltered half2 map from Relion's refine3d.

Fileemd_23050_half_map_2.map
AnnotationUnfiltered half2 map from Relion's refine3d.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Hsp90-Hsp70-Hop-GR complex

EntireName: Hsp90-Hsp70-Hop-GR complex
Components
  • Complex: Hsp90-Hsp70-Hop-GR complex
    • Complex: Heat shock protein HSP 90-alphaHeat shock response
      • Protein or peptide: Heat shock protein HSP 90-alphaHeat shock response
    • Complex: Heat shock 70 kDa protein 1A
      • Protein or peptide: Heat shock 70 kDa protein 1A
    • Complex: Stress-induced-phosphoprotein 1
      • Protein or peptide: Stress-induced-phosphoprotein 1
    • Complex: Glucocorticoid receptor
      • Protein or peptide: Glucocorticoid receptor
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: POTASSIUM IONPotassium

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Supramolecule #1: Hsp90-Hsp70-Hop-GR complex

SupramoleculeName: Hsp90-Hsp70-Hop-GR complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4

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Supramolecule #2: Heat shock protein HSP 90-alpha

SupramoleculeName: Heat shock protein HSP 90-alpha / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Heat shock 70 kDa protein 1A

SupramoleculeName: Heat shock 70 kDa protein 1A / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: Stress-induced-phosphoprotein 1

SupramoleculeName: Stress-induced-phosphoprotein 1 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #5: Glucocorticoid receptor

SupramoleculeName: Glucocorticoid receptor / type: complex / ID: 5 / Parent: 1 / Macromolecule list: #4
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Heat shock protein HSP 90-alpha

MacromoleculeName: Heat shock protein HSP 90-alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 84.781727 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTL TIVDTGIGMT KADLINNLGT IAKSGTKAFM EALQAGADIS MIGQFGVGFY SAYLVAEKVT VITKHNDDEQ Y AWESSAGG ...String:
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTL TIVDTGIGMT KADLINNLGT IAKSGTKAFM EALQAGADIS MIGQFGVGFY SAYLVAEKVT VITKHNDDEQ Y AWESSAGG SFTVRTDTGE PMGRGTKVIL HLKEDQTEYL EERRIKEIVK KHSQFIGYPI TLFVEKERDK EVSDDEAEEK ED KEEEKEK EEKESEDKPE IEDVGSDEEE EKKDGDKKKK KKIKEKYIDQ EELNKTKPIW TRNPDDITNE EYGEFYKSLT NDW EDHLAV KHFSVEGQLE FRALLFVPRR APFDLFENRK KKNNIKLYVR RVFIMDNCEE LIPEYLNFIR GVVDSEDLPL NISR EMLQQ SKILKVIRKN LVKKCLELFT ELAEDKENYK KFYEQFSKNI KLGIHEDSQN RKKLSELLRY YTSASGDEMV SLKDY CTRM KENQKHIYYI TGETKDQVAN SAFVERLRKH GLEVIYMIEP IDEYCVQQLK EFEGKTLVSV TKEGLELPED EEEKKK QEE KKTKFENLCK IMKDILEKKV EKVVVSNRLV TSPCCIVTST YGWTANMERI MKAQALRDNS TMGYMAAKKH LEINPDH SI IETLRQKAEA DKNDKSVKDL VILLYETALL SSGFSLEDPQ THANRIYRMI KLGLGIDEDD PTADDTSAAV TEEMPPLE G DDDTSRMEEV D

UniProtKB: Heat shock protein HSP 90-alpha

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Macromolecule #2: Heat shock 70 kDa protein 1A

MacromoleculeName: Heat shock 70 kDa protein 1A / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 70.140133 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKH WPFQVINDGD KPKVQVSYKG ETKAFYPEEI SSMVLTKMKE IAEAYLGYPV TNAVITVPAY FNDSQRQATK D AGVIAGLN ...String:
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKH WPFQVINDGD KPKVQVSYKG ETKAFYPEEI SSMVLTKMKE IAEAYLGYPV TNAVITVPAY FNDSQRQATK D AGVIAGLN VLRIINEPTA AAIAYGLDRT GKGERNVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV NH FVEEFKR KHKKDISQNK RAVRRLRTAC ERAKRTLSSS TQASLEIDSL FEGIDFYTSI TRARFEELCS DLFRSTLEPV EKA LRDAKL DKAQIHDLVL VGGSTRIPKV QKLLQDFFNG RDLNKSINPD EAVAYGAAVQ AAILMGDKSE NVQDLLLLDV APLS LGLET AGGVMTALIK RNSTIPTKQT QIFTTYSDNQ PGVLIQVYEG ERAMTKDNNL LGRFELSGIP PAPRGVPQIE VTFDI DANG ILNVTATDKS TGKANKITIT NDKGRLSKEE IERMVQEAEK YKAEDEVQRE RVSAKNALES YAFNMKSAVE DEGLKG KIS EADKKKVLDK CQEVISWLDA NTLAEKDEFE HKRKELEQVC NPIISGLYQG AGGPGPGGFG AQGPKGGSGS GPTIEEV D

UniProtKB: Heat shock 70 kDa protein 1A

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Macromolecule #3: Stress-induced-phosphoprotein 1

MacromoleculeName: Stress-induced-phosphoprotein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 62.738301 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFE EAKRTYEEGL KHEANNPQLK EGLQNMEARL AERKFMNPFN MPNLYQKLES DPRTRTLLSD PTYRELIEQL R NKPSDLGT ...String:
MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFE EAKRTYEEGL KHEANNPQLK EGLQNMEARL AERKFMNPFN MPNLYQKLES DPRTRTLLSD PTYRELIEQL R NKPSDLGT KLQDPRIMTT LSVLLGVDLG SMDEEEEIAT PPPPPPPKKE TKPEPMEEDL PENKKQALKE KELGNDAYKK KD FDTALKH YDKAKELDPT NMTYITNQAA VYFEKGDYNK CRELCEKAIE VGRENREDYR QIAKAYARIG NSYFKEEKYK DAI HFYNKS LAEHRTPDVL KKCQQAEKIL KEQERLAYIN PDLALEEKNK GNECFQKGDY PQAMKHYTEA IKRNPKDAKL YSNR AACYT KLLEFQLALK DCEECIQLEP TFIKGYTRKA AALEAMKDYT KAMDVYQKAL DLDSSCKEAA DGYQRCMMAQ YNRHD SPED VKRRAMADPE VQQIMSDPAM RLILEQMQKD PQALSEHLKN PVIAQKIQKL MDVGLIAIR

UniProtKB: Stress-induced-phosphoprotein 1

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Macromolecule #4: Glucocorticoid receptor

MacromoleculeName: Glucocorticoid receptor / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 85.673906 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MDSKESLTPG REENPSSVLA QERGDVMDFY KTLRGGATVK VSASSPSLAV ASQSDSKQRR LLVDFPKGSV SNAQQPDLSK AVSLSMGLY MGETETKVMG NDLGFPQQGQ ISLSSGETDL KLLEESIANL NRSTSVPENP KSSASTAVSA APTEKEFPKT H SDVSSEQQ ...String:
MDSKESLTPG REENPSSVLA QERGDVMDFY KTLRGGATVK VSASSPSLAV ASQSDSKQRR LLVDFPKGSV SNAQQPDLSK AVSLSMGLY MGETETKVMG NDLGFPQQGQ ISLSSGETDL KLLEESIANL NRSTSVPENP KSSASTAVSA APTEKEFPKT H SDVSSEQQ HLKGQTGTNG GNVKLYTTDQ STFDILQDLE FSSGSPGKET NESPWRSDLL IDENCLLSPL AGEDDSFLLE GN SNEDCKP LILPDTKPKI KDNGDLVLSS PSNVTLPQVK TEKEDFIELC TPGVIKQEKL GTVYCQASFP GANIIGNKMS AIS VHGVST SGGQMYHYDM NTASLSQQQD QKPIFNVIPP IPVGSENWNR CQGSGDDNLT SLGTLNFPGR TVFSNGYSSP SMRP DVSSP PSSSSTATTG PPPKLCLVCS DEASGCHYGV LTCGSCKVFF KRAVEGQHNY LCAGRNDCII DKIRRKNCPA CRYRK CLQA GMNLEARKTK KKIKGIQQAT TGVSQETSEN PGNKSIVPAT LPQLTPTLVS LLEVIEPEVL YAGYDSSVPD STWRIM TTL NMLGGRQVIA AVKWAKAIPG FRNLHLDDQM TLLQYSWMSL MAFALGWRSY RQSSANLLCF APDLIINEQR MTLPCMY DQ CKHMLYVSSE LHRLQVSYEE YLCMKTLLLL SSVPKDGLKS QELFDEIRMT YIKELGKAIV KREGNSSQNW QRFYQLTK L LDSMHEVVEN LLNYCFQTFL DKTMSIEFPE MLAEIITNQI PKYSNGNIKK LLFHQK

UniProtKB: Glucocorticoid receptor

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Macromolecule #5: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

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Macromolecule #6: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #7: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 7 / Number of copies: 2 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 80.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Details: The Hsp90 semi-open conformation from the Hsp90:Hop cryo-EM structure from Southworth & Agard (2011).
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final 3D classificationNumber classes: 4
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.57 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 85619
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT / Overall B value: 80
Output model

PDB-7kw7:
Atomic cryoEM structure of Hsp90-Hsp70-Hop-GR

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