+Open data
-Basic information
Entry | Database: PDB / ID: 7y04 | ||||||
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Title | Hsp90-AhR-p23 complex | ||||||
Components |
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Keywords | CYTOSOLIC 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 / negative regulation of T cell mediated immune response to tumor cell / cytosolic aryl hydrocarbon receptor complex / glomerulus morphogenesis / DDX58/IFIH1-mediated induction of interferon-alpha/beta / The NLRP3 inflammasome ...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 / negative regulation of T cell mediated immune response to tumor cell / cytosolic aryl hydrocarbon receptor complex / glomerulus morphogenesis / DDX58/IFIH1-mediated induction of interferon-alpha/beta / The NLRP3 inflammasome / gland development / HSF1-dependent transactivation / regulation of B cell proliferation / 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 / cellular response to molecule of bacterial origin / ooplasm / omega-hydroxylase P450 pathway / Sema3A PAK dependent Axon repulsion / prostaglandin-E synthase / prostaglandin-E synthase activity / arachidonic acid omega-hydroxylase activity / central nervous system neuron axonogenesis / positive regulation of growth rate / lymphocyte homeostasis / Attenuation phase / regulation of adaptive immune response / : / : / 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 / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / HSP90-CDC37 chaperone complex / positive regulation of cyclin-dependent protein kinase activity / intracellular glucocorticoid receptor signaling pathway / cardiac left ventricle morphogenesis / The role of GTSE1 in G2/M progression after G2 checkpoint / sperm head plasma membrane / negative regulation of proteasomal protein catabolic process / negative regulation of osteoblast proliferation / cellular response to toxic substance / reproductive structure development / prostate gland development / aryl hydrocarbon receptor complex / dynein axonemal particle / Regulation of actin dynamics for phagocytic cup formation / histone methyltransferase binding / B-1 B cell homeostasis / Estrogen-dependent gene expression / post-embryonic hemopoiesis / COP9 signalosome / positive regulation of protein localization to cell surface / negative regulation of DNA biosynthetic process / ATP-dependent protein binding / camera-type eye development / vasculature development / axon extension / telomerase holoenzyme complex / negative regulation of systemic arterial blood pressure / glycogen biosynthetic process / protein folding chaperone complex / blood circulation / blood vessel morphogenesis / prostaglandin biosynthetic process / dATP binding / sulfonylurea receptor binding / CTP binding / negative regulation of protein metabolic process / skin development / UTP binding / negative regulation of vasoconstriction / branching involved in blood vessel morphogenesis / telomerase holoenzyme complex assembly / immune system process / establishment of cell polarity / prostaglandin metabolic process / heterocyclic compound binding / blood vessel development / TPR domain binding / E-box binding / T cell homeostasis / positive regulation of transforming growth factor beta receptor signaling pathway / dendritic growth cone / chaperone cofactor-dependent protein refolding / positive regulation of phosphoprotein phosphatase activity / TFIID-class transcription factor complex binding / aryl hydrocarbon receptor binding / B cell homeostasis / cAMP-mediated signaling / regulation of protein ubiquitination Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
Authors | Wen, Z.L. / Zhai, Y.J. / Zhu, Y. / Sun, F. | ||||||
Funding support | 1items
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Citation | Journal: 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7y04.cif.gz | 281.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7y04.ent.gz | 222.1 KB | Display | PDB format |
PDBx/mmJSON format | 7y04.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y0/7y04 ftp://data.pdbj.org/pub/pdb/validation_reports/y0/7y04 | HTTPS FTP |
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-Related structure data
Related structure data | 33537MC 8h77C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | 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 | 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 | | 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 | #5: Chemical | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
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Buffer solution | pH: 7.5 | |||||||||||||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2000 nm / Nominal defocus min: 1300 nm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 291578 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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