+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-33537 | |||||||||
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Title | Hsp90-AhR-p23 complex | |||||||||
Map data | Hsp90-AhR-p23 complex | |||||||||
Sample |
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Keywords | Hsp90 / AhR / complex / p23 / CYTOSOLIC PROTEIN | |||||||||
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 | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Wen ZL / Zhai YJ / Zhu Y / Sun F | |||||||||
Funding support | 1 items
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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
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_33537.map.gz | 59.6 MB | EMDB map data format | |
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Header (meta data) | emd-33537-v30.xml emd-33537.xml | 18.6 KB 18.6 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_33537_fsc.xml | 9.1 KB | Display | FSC data file |
Images | emd_33537.png | 15 KB | ||
Filedesc metadata | emd-33537.cif.gz | 6.3 KB | ||
Others | emd_33537_half_map_1.map.gz emd_33537_half_map_2.map.gz | 59.5 MB 59.5 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-33537 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-33537 | HTTPS FTP |
-Related structure data
Related structure data | 7y04MC 8h77C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_33537.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | Hsp90-AhR-p23 complex | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_33537_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_33537_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Hsp90-AhR-p23 complex
Entire | Name: Hsp90-AhR-p23 complex |
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Components |
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-Supramolecule #1: Hsp90-AhR-p23 complex
Supramolecule | Name: Hsp90-AhR-p23 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: Mus musculus (house mouse) |
-Supramolecule #2: Heat shock protein HSP 90-beta
Supramolecule | Name: Heat shock protein HSP 90-beta / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: Mus musculus (house mouse) |
-Supramolecule #3: Prostaglandin E synthase 3
Supramolecule | Name: Prostaglandin E synthase 3 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 / Details: also named p23 |
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Source (natural) | Organism: Mus musculus (house mouse) |
-Supramolecule #4: Aryl hydrocarbon receptor
Supramolecule | Name: Aryl hydrocarbon receptor / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3 |
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-Macromolecule #1: Heat shock protein HSP 90-beta
Macromolecule | Name: Heat shock protein HSP 90-beta / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 86.590688 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MGAWSHPQFE KGGGSGGGSG GGSAWSHPQF EKMPEEVHHG EEEVETFAFQ AEIAQLMSLI INTFYSNKEI FLRELISNAS DALDKIRYE SLTDPSKLDS GKELKIDIIP NPQERTLTLV DTGIGMTKAD LINNLGTIAK SGTKAFMEAL QAGADISMIG Q FGVGFYSA ...String: MGAWSHPQFE KGGGSGGGSG GGSAWSHPQF EKMPEEVHHG EEEVETFAFQ AEIAQLMSLI INTFYSNKEI FLRELISNAS DALDKIRYE SLTDPSKLDS GKELKIDIIP NPQERTLTLV DTGIGMTKAD LINNLGTIAK SGTKAFMEAL QAGADISMIG Q FGVGFYSA YLVAEKVVVI TKHNDDEQYA WESSAGGSFT VRADHGEPIG RGTKVILHLK EDQTEYLEER RVKEVVKKHS QF IGYPITL YLEKEREKEI SDDEAEEEKG EKEEEDKEDE EKPKIEDVGS DEEDDSGKDK KKKTKKIKEK YIDQEELNKT KPI WTRNPD DITQEEYGEF YKSLTNDWED HLAVKHFSVE GQLEFRALLF IPRRAPFDLF ENKKKKNNIK LYVRRVFIMD SCDE LIPEY LNFIRGVVDS EDLPLNISRE MLQQSKILKV IRKNIVKKCL ELFSELAEDK ENYKKFYEAF SKNLKLGIHE DSTNR RRLS ELLRYHTSQS GDEMTSLSEY VSRMKETQKS IYYITGESKE QVANSAFVER VRKRGFEVVY MTEPIDEYCV QQLKEF DGK SLVSVTKEGL ELPEDEEEKK KMEESKAKFE NLCKLMKEIL DKKVEKVTIS NRLVSSPCCI VTSTYGWTAN MERIMKA QA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGL G IDEDEVTAEE PSAAVPDEIP PLEGDEDASR MEEVD UniProtKB: Heat shock protein HSP 90-beta |
-Macromolecule #2: Prostaglandin E synthase 3
Macromolecule | Name: Prostaglandin E synthase 3 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: prostaglandin-E synthase |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 20.133994 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MAEQKLISEE DLMQPASAKW YDRRDYVFIE FCVEDSKDVN VNFEKSKLTF SCLGGSDNFK HLNEIDLFHC IDPNDSKHKR TDRSILCCL RKGESGQSWP RLTKERAKLN WLSVDFNNWK DWEDDSDEDM SNFDRFSEMM DHMGGDEDVD LPEVDGADDD S QDSDDEKM PDLE UniProtKB: Prostaglandin E synthase 3 |
-Macromolecule #3: Aryl hydrocarbon receptor
Macromolecule | Name: Aryl hydrocarbon receptor / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 46.138473 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: GPGASGGGSG AGMSSGANIT YASRKRRKPV QKTVKPIPAE GIKSNPSKRH RDRLNTELDR LASLLPFPQD VINKLDKLSV LRLSVSYLR AKSFFDVALK STPADRNGGQ DQCRAQIRDW QDLQEGEFLL QALNGFVLVV TADALVFYAS STIQDYLGFQ Q SDVIHQSV ...String: GPGASGGGSG AGMSSGANIT YASRKRRKPV QKTVKPIPAE GIKSNPSKRH RDRLNTELDR LASLLPFPQD VINKLDKLSV LRLSVSYLR AKSFFDVALK STPADRNGGQ DQCRAQIRDW QDLQEGEFLL QALNGFVLVV TADALVFYAS STIQDYLGFQ Q SDVIHQSV YELIHTEDRA EFQRQLHWAL NPDSAQGVDE AHGPPQAAVY YTPDQLPPEN ASFMERCFRC RLRCLLDNSS GF LAMNFQG RLKYLHGQNK KGKDGALLPP QLALFAIATP LQPPSILEIR TKNFIFRTKH KLDFTPIGCD AKGQLILGYT EVE LCTRGS GYQFIHAADM LHCAESHIRM IKTGESGMTV FRLFAKHSRW RWVQSNARLI YRNGRPDYII ATQRPLTDEE GREH LQKRS TSLPF UniProtKB: Aryl hydrocarbon receptor |
-Macromolecule #4: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 2 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ChemComp-ADP: |
-Macromolecule #5: BERYLLIUM TRIFLUORIDE ION
Macromolecule | Name: BERYLLIUM TRIFLUORIDE ION / type: ligand / ID: 5 / Number of copies: 2 / Formula: BEF |
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Molecular weight | Theoretical: 66.007 Da |
Chemical component information | ChemComp-BEF: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.3 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |