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- PDB-7y04: Hsp90-AhR-p23 complex -

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Basic information

Entry
Database: PDB / ID: 7y04
TitleHsp90-AhR-p23 complex
Components
  • Aryl hydrocarbon receptor
  • Heat shock protein HSP 90-beta
  • Prostaglandin E synthase 3
KeywordsCYTOSOLIC PROTEIN / Hsp90 / AhR / complex / p23
Function / homology
Function and homology information


circumferential growth involved in left ventricle morphogenesis / negative regulation of calcium ion transmembrane transport / cellular response to 3-methylcholanthrene / regulation of heart growth / ESR-mediated signaling / cytosolic aryl hydrocarbon receptor complex / glomerulus morphogenesis / DDX58/IFIH1-mediated induction of interferon-alpha/beta / The NLRP3 inflammasome / gland development ...circumferential growth involved in left ventricle morphogenesis / negative regulation of calcium ion transmembrane transport / cellular response to 3-methylcholanthrene / regulation of heart growth / ESR-mediated signaling / cytosolic aryl hydrocarbon receptor complex / glomerulus morphogenesis / DDX58/IFIH1-mediated induction of interferon-alpha/beta / The NLRP3 inflammasome / gland development / HSF1-dependent transactivation / reactive oxygen species biosynthetic process / Phase I - Functionalization of compounds / Xenobiotics / Aryl hydrocarbon receptor signalling / HSF1 activation / kidney morphogenesis / RHOBTB2 GTPase cycle / lung saccule development / ooplasm / Sema3A PAK dependent Axon repulsion / omega-hydroxylase P450 pathway / prostaglandin-E synthase / prostaglandin-E synthase activity / arachidonate omega-hydroxylase activity / positive regulation of growth rate / Attenuation phase / lymphocyte homeostasis / regulation of adaptive immune response / receptor ligand inhibitor activity / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / negative regulation of complement-dependent cytotoxicity / cellular response to 2,3,7,8-tetrachlorodibenzodioxine / telomerase activity / Endogenous sterols / nuclear aryl hydrocarbon receptor complex / HSP90-CDC37 chaperone complex / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / nuclear receptor-mediated glucocorticoid signaling pathway / sperm head plasma membrane / cardiac left ventricle morphogenesis / The role of GTSE1 in G2/M progression after G2 checkpoint / negative regulation of proteasomal protein catabolic process / negative regulation of osteoblast proliferation / prostate gland development / reproductive structure development / cellular response to toxic substance / aryl hydrocarbon receptor complex / negative regulation of T cell mediated immune response to tumor cell / Regulation of actin dynamics for phagocytic cup formation / dynein axonemal particle / histone methyltransferase binding / B-1 B cell homeostasis / Estrogen-dependent gene expression / COP9 signalosome / post-embryonic hemopoiesis / E-box binding / negative regulation of DNA biosynthetic process / positive regulation of protein localization to cell surface / ATP-dependent protein binding / vasculature development / camera-type eye development / negative regulation of systemic arterial blood pressure / telomerase holoenzyme complex / blood circulation / glycogen biosynthetic process / protein folding chaperone complex / negative regulation of protein metabolic process / blood vessel morphogenesis / prostaglandin biosynthetic process / dATP binding / sulfonylurea receptor binding / CTP binding / UTP binding / skin development / negative regulation of vasoconstriction / telomerase holoenzyme complex assembly / branching involved in blood vessel morphogenesis / immune system process / prostaglandin metabolic process / negative regulation of osteoblast differentiation / heterocyclic compound binding / TPR domain binding / blood vessel development / positive regulation of transforming growth factor beta receptor signaling pathway / T cell homeostasis / dendritic growth cone / positive regulation of phosphorylation / aryl hydrocarbon receptor binding / B cell homeostasis / : / regulation of protein ubiquitination / chaperone cofactor-dependent protein refolding / telomere maintenance via telomerase / positive regulation of cell size / protein localization to nucleus / chaperone-mediated protein complex assembly / toxic substance binding / positive regulation of RNA polymerase II transcription preinitiation complex assembly / blood vessel remodeling
Similarity search - Function
Aryl hydrocarbon receptor / Aryl hydrocarbon receptor/Aryl hydrocarbon receptor repressor / Co-chaperone protein p23-like / CS domain / CS domain / CS domain profile. / PAS fold-3 / PAS fold / HSP20-like chaperone / Helix-loop-helix DNA-binding domain ...Aryl hydrocarbon receptor / Aryl hydrocarbon receptor/Aryl hydrocarbon receptor repressor / Co-chaperone protein p23-like / CS domain / CS domain / CS domain profile. / PAS fold-3 / PAS fold / HSP20-like chaperone / Helix-loop-helix DNA-binding domain / PAC motif / Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) / 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 / Helix-loop-helix DNA-binding domain superfamily / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / PAS fold / PAS fold / PAS domain / PAS repeat profile. / PAS domain / Histidine kinase-like ATPases / PAS domain superfamily / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / BERYLLIUM TRIFLUORIDE ION / Heat shock protein HSP 90-beta / Aryl hydrocarbon receptor / Prostaglandin E synthase 3
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsWen, Z.L. / Zhai, Y.J. / Zhu, Y. / Sun, F.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Structure / Year: 2023
Title: Cryo-EM structure of the cytosolic AhR complex.
Authors: Zuoling Wen / Yuebin Zhang / Beirong Zhang / Yumo Hang / Li Xu / Yangsheng Chen / Qunhui Xie / Qun Zhao / Lihua Zhang / Guohui Li / Bin Zhao / Fei Sun / Yujia Zhai / Yun Zhu /
Abstract: Aryl hydrocarbon receptor (AhR) is an important ligand-activated transcription factor involved in the regulation of various important physiological functions. Here, we report the cryo-EM structures ...Aryl hydrocarbon receptor (AhR) is an important ligand-activated transcription factor involved in the regulation of various important physiological functions. Here, we report the cryo-EM structures of the Hsp90-AhR-p23 complex with or without bound XAP2, where the structure of the mouse AhR PAS-B domain is resolved. A highly conserved bridge motif of AhR is responsible for the interaction with the Hsp90 dimeric lumen. The ligand-free AhR PAS-B domain is attached to the Hsp90 dimer and is stabilized in the complex with bound XAP2. In addition, the DE-loop and a group of conserved pocket inner residues in the AhR PAS-B domain are found to be important for ligand binding. These results reveal the structural basis of the biological functions of AhR. Moreover, the protein purification method presented here allows the isolation of stable mouse AhR protein, which could be used to develop high-sensitivity biosensors for environmental pollutant detection.
History
DepositionJun 3, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 4, 2023Provider: repository / Type: Initial release
Revision 1.1Jan 25, 2023Group: Database references / Category: citation / citation_author / Item: _citation.pdbx_database_id_DOI
Revision 1.2Feb 1, 2023Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.3Mar 22, 2023Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.page_first
Revision 1.4Jul 3, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond / em_admin / Item: _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Heat shock protein HSP 90-beta
B: Heat shock protein HSP 90-beta
C: Prostaglandin E synthase 3
D: Prostaglandin E synthase 3
E: Aryl hydrocarbon receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)260,5749
Polymers259,5885
Non-polymers9864
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Heat shock protein HSP 90-beta / Heat shock 84 kDa / HSP 84 / HSP84 / Tumor-specific transplantation 84 kDa antigen / TSTA


Mass: 86590.688 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Hsp90ab1, Hsp84, Hsp84-1, Hspcb / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P11499
#2: Protein Prostaglandin E synthase 3 / Cytosolic prostaglandin E2 synthase / cPGES / Hsp90 co-chaperone / Progesterone receptor complex ...Cytosolic prostaglandin E2 synthase / cPGES / Hsp90 co-chaperone / Progesterone receptor complex p23 / Sid 3177 / Telomerase-binding protein p23


Mass: 20133.994 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ptges3, Sid3177, Tebp / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9R0Q7, prostaglandin-E synthase
#3: Protein Aryl hydrocarbon receptor


Mass: 46138.473 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P30561
#4: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#5: Chemical ChemComp-BEF / BERYLLIUM TRIFLUORIDE ION


Mass: 66.007 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: BeF3
Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

Component
IDNameTypeEntity IDParent-IDSourceDetails
1Hsp90-AhR-p23 complexCOMPLEX#1-#30RECOMBINANT
2Heat shock protein HSP 90-betaCOMPLEX#11RECOMBINANT
3Prostaglandin E synthase 3COMPLEX#21RECOMBINANTalso named p23
4Aryl hydrocarbon receptorCOMPLEX#31RECOMBINANT
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
21Mus musculus (house mouse)10090
32Mus musculus (house mouse)10090
43Mus musculus (house mouse)10090
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
21Spodoptera frugiperda (fall armyworm)7108
32Spodoptera frugiperda (fall armyworm)7108
43Spodoptera frugiperda (fall armyworm)7108
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1300 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.19.2_4158: / Classification: refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 291578 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00212253
ELECTRON MICROSCOPYf_angle_d0.54116495
ELECTRON MICROSCOPYf_dihedral_angle_d4.881599
ELECTRON MICROSCOPYf_chiral_restr0.0431810
ELECTRON MICROSCOPYf_plane_restr0.0042105

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