+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-28609 | |||||||||
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Title | Class1 of the INO80-Nucleosome complex | |||||||||
Map data | Class1,INO80-Ncp,overall | |||||||||
Sample |
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Keywords | Chromatin Remodeler / hexasome / DNA BINDING PROTEIN / DNA BINDING PROTEIN-Hydrolase complex | |||||||||
Function / homology | Function and homology information R2TP complex / regulation of TOR signaling / Swr1 complex / telomere maintenance via recombination / Ino80 complex / regulation of metabolic process / box C/D snoRNP assembly / DNA duplex unwinding / ATP-dependent chromatin remodeler activity / 3'-5' DNA helicase activity ...R2TP complex / regulation of TOR signaling / Swr1 complex / telomere maintenance via recombination / Ino80 complex / regulation of metabolic process / box C/D snoRNP assembly / DNA duplex unwinding / ATP-dependent chromatin remodeler activity / 3'-5' DNA helicase activity / NuA4 histone acetyltransferase complex / chromosome, centromeric region / subtelomeric heterochromatin formation / enzyme regulator activity / DNA helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / rRNA processing / histone binding / 5'-3' DNA helicase activity / DNA helicase / transcription by RNA polymerase II / chromosome, telomeric region / protein stabilization / chromatin remodeling / DNA repair / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / ATP binding / nucleus / cytoplasm Similarity search - Function | |||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) / Saccharomyces cerevisiae S288C (yeast) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.48 Å | |||||||||
Authors | Wu H / Munoz E / Gourdet M / Cheng YF / Narlikar G | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Science / Year: 2023 Title: Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility. Authors: Hao Wu / Elise N Muñoz / Laura J Hsieh / Un Seng Chio / Muryam A Gourdet / Geeta J Narlikar / Yifan Cheng / Abstract: Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report ...Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of INO80 bound to a hexasome or a nucleosome. INO80 binds the two substrates in substantially different orientations. On a hexasome, INO80 places its ATPase subunit, Ino80, at superhelical location -2 (SHL -2), in contrast to SHL -6 and SHL -7, as previously seen on nucleosomes. Our results suggest that INO80 action on hexasomes resembles action by other remodelers on nucleosomes such that Ino80 is maximally active near SHL -2. The SHL -2 position also plays a critical role for nucleosome remodeling by INO80. Overall, the mechanistic adaptations used by INO80 for preferential hexasome sliding imply that subnucleosomal particles play considerable regulatory roles. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_28609.map.gz | 210.3 MB | EMDB map data format | |
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Header (meta data) | emd-28609-v30.xml emd-28609.xml | 22.6 KB 22.6 KB | Display Display | EMDB header |
Images | emd_28609.png | 135.6 KB | ||
Filedesc metadata | emd-28609.cif.gz | 6.9 KB | ||
Others | emd_28609_additional_1.map.gz emd_28609_half_map_1.map.gz emd_28609_half_map_2.map.gz | 49.8 MB 263.3 MB 263.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-28609 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-28609 | HTTPS FTP |
-Validation report
Summary document | emd_28609_validation.pdf.gz | 820.9 KB | Display | EMDB validaton report |
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Full document | emd_28609_full_validation.pdf.gz | 820.5 KB | Display | |
Data in XML | emd_28609_validation.xml.gz | 17.3 KB | Display | |
Data in CIF | emd_28609_validation.cif.gz | 20.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28609 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28609 | HTTPS FTP |
-Related structure data
Related structure data | 8eu9MC 8etsC 8ettC 8etuC 8etvC 8etwC 8eu2C 8eueC 8eufC 8eujC 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_28609.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Class1,INO80-Ncp,overall | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.835 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Class1,INO80-Ncp,ncp
File | emd_28609_additional_1.map | ||||||||||||
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Annotation | Class1,INO80-Ncp,ncp | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Class1,INO80-Ncp,overall,halfmap1
File | emd_28609_half_map_1.map | ||||||||||||
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Annotation | Class1,INO80-Ncp,overall,halfmap1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Class1,INO80-Ncp,overall,halfmap2
File | emd_28609_half_map_2.map | ||||||||||||
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Annotation | Class1,INO80-Ncp,overall,halfmap2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : INO80-Ncp
Entire | Name: INO80-Ncp |
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Components |
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-Supramolecule #1: INO80-Ncp
Supramolecule | Name: INO80-Ncp / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6 |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
-Macromolecule #1: Chromatin-remodeling ATPase INO80
Macromolecule | Name: Chromatin-remodeling ATPase INO80 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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Source (natural) | Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 56.002078 KDa |
Sequence | String: IEIDVLCDLT QRQAKLYQVL KSQISTNYDA IENAATNDST SNSASNSGSD QNLINAVMQF RKVCNHPDLF ERADVDSPFS FTTFGKTTS MLTASVANNN SSVISNSNMN LSSMSSNNIS NGKFTDLIYS SRNPIKYSLP RLIYEDLILP NYNNDVDIAN K LKNVKFNI ...String: IEIDVLCDLT QRQAKLYQVL KSQISTNYDA IENAATNDST SNSASNSGSD QNLINAVMQF RKVCNHPDLF ERADVDSPFS FTTFGKTTS MLTASVANNN SSVISNSNMN LSSMSSNNIS NGKFTDLIYS SRNPIKYSLP RLIYEDLILP NYNNDVDIAN K LKNVKFNI FNPSTNYELC LFLSKLTGEP SLNEFFRVST TPLLKRVIER TNGPKNTDSL SFKTITQELL EVTRNAPSEG VM ASLLNVE KHAYEREYLN CIQRGYHPNV SAPPVTIEVL GSSHVTNSIN NELFDPLISQ ALSDIPAITQ YNMHVKKGIP VED FPKTGL FPEPLNKNFS SNISMPSMDR FITESAKLRK LDELLVKLKS EGHRVLIYFQ MTKMMDLMEE YLTYRQYNHI RLDG SSKLE DRRDLVHDWQ TNPEIFVFLL STRAGGLGIN LTAADTVIFY DSDWNPTIDS QAMDRAHRLG QTRQVTVYRL LVRGT IEER MRDRAKQKE UniProtKB: Chromatin-remodeling ATPase INO80 |
-Macromolecule #2: Actin-related protein 5
Macromolecule | Name: Actin-related protein 5 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 87.682359 KDa |
Sequence | String: MSSRDASLTP LKAVVIDDPP LRQTPEPFDE QSAYNPQSPI AIDFGSSKLR AGFVNHATPT HIFPNALTKF RDRKLNKNFT FVGNDTLLD QAVRSQSRSP FDGPFVTNWN LTEEILDYTF HHLGVVPDNG IPNPILLTER LATVQSQRTN WYQILFETYN V PGVTFGID ...String: MSSRDASLTP LKAVVIDDPP LRQTPEPFDE QSAYNPQSPI AIDFGSSKLR AGFVNHATPT HIFPNALTKF RDRKLNKNFT FVGNDTLLD QAVRSQSRSP FDGPFVTNWN LTEEILDYTF HHLGVVPDNG IPNPILLTER LATVQSQRTN WYQILFETYN V PGVTFGID SLFSFYNYNP SGNKTGLVIS CGHEDTNVIP VVDGAGILTD AKRINWGGHQ AVDYLNDLMA LKYPYFPTKM SY LQYETMY KDYCYVSRNY DEDIEKILTL ENLDTNDVVV EAPFTEVLQP QKTEEELRIQ AEKRKETGKR LQEQARLKRM EKL VQKQEE FEYFSKVRDQ LIDEPKKKVL SVLQNAGFDD ERDFKKYLHS LEQSLKKAQM VEAEDDSHLD EMNEDKTAQK FDLL DIADE DLNEDQIKEK RKQRFLKASQ DARQKAKEEK ERVAKEEEEK KLKEQQWRET DLNGWIKDKR LKLNKLIKRR KEKLK LRDE MKDRKSQVSQ NRMKNLASLA EDNVKQGAKR NRHQATIDND PNDTFGANDE DWLIYTDITQ NPEAFEEALE YEYKDI VEL ERLLLEHDPN FTEEDTLEAQ YDWRNSILHL FLRGPRPHDS ENIHEQHQMH LNVERIRVPE VIFQPTMGGQ DQAGICE LS ETILLKKFGS QPGKLSQTSI DMVNNVLITG GNAKVPGLKE RIVKEFTGFL PTGTNITVNM SSDPSLDAWK GMAALARN E EQYRKTVISK KEYEEYGPEY IKEHKLGNTK YFED UniProtKB: Actin-related protein 5 |
-Macromolecule #3: Chromatin-remodeling complex subunit IES6
Macromolecule | Name: Chromatin-remodeling complex subunit IES6 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 15.392762 KDa |
Sequence | String: ERLLFLRSVG ERNEIGFPSR FKSAHYKKPT RRHKSARQLI SDENKRINAL LTKANKAAES STAARRLVPK ATYFSVEAPP SIRPAKKYC DVTGLKGFYK SPTNNIRYHN AEIYQLIVKP MAPGVDQEYL KLRGAN UniProtKB: Chromatin-remodeling complex subunit IES6 |
-Macromolecule #4: RuvB-like protein 1
Macromolecule | Name: RuvB-like protein 1 / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase |
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Source (natural) | Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 48.543805 KDa |
Sequence | String: VTRTAAHTHI KGLGLDESGV AKRVEGGFVG QIEAREACGV IVDLIKAKKM SGRAILLAGG PSTGKTALAL AISQELGPKV PFCPLVGSE LYSVEVKKTE TLMENFRRAI GLRIKETKEV YEGEVTELTP EDAENPLGGY GKTISHVIVG LKSAKGTKTL R LDPTIYES ...String: VTRTAAHTHI KGLGLDESGV AKRVEGGFVG QIEAREACGV IVDLIKAKKM SGRAILLAGG PSTGKTALAL AISQELGPKV PFCPLVGSE LYSVEVKKTE TLMENFRRAI GLRIKETKEV YEGEVTELTP EDAENPLGGY GKTISHVIVG LKSAKGTKTL R LDPTIYES IQREKVSIGD VIYIEANTGA VKRVGRSDAY ATEFDLETEE YVPLPKGEVH KKKEIVQDVT LHDLDVANAR PQ GGQDVIS MMGQLLKPKK TEITEKLRQE VNKVVAKYID QGVAELIPGV LFIDEVNMLD IEIFTYLNKA LESNIAPVVV LAS NRGMTT VRGTEDVISP HGVPPDLIDR LLIVRTLPYD KDEIRTIIER RATVERLQVE SSALDLLATM GTETSLRYAL QLLA PCGIL AQTSNRKEIV VNDVNEAKLL FLDAKRSTKI LETSANYL UniProtKB: RuvB-like protein 1 |
-Macromolecule #5: RuvB-like protein 2
Macromolecule | Name: RuvB-like protein 2 / type: protein_or_peptide / ID: 5 / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase |
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Source (natural) | Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 49.019773 KDa |
Sequence | String: KSLSLIAAHS HITGLGLDEN LQPRPTSEGM VGQLQARRAA GVILKMVQNG TIAGRAVLVA GPPSTGKTAL AMGVSQSLGK DVPFTAIAG SEIFSLELSK TEALTQAFRK SIGIKIKEET ELIEGEVVEI QIDRSITGGH KQGKLTIKTT DMETIYELGN K MIDGLTKE ...String: KSLSLIAAHS HITGLGLDEN LQPRPTSEGM VGQLQARRAA GVILKMVQNG TIAGRAVLVA GPPSTGKTAL AMGVSQSLGK DVPFTAIAG SEIFSLELSK TEALTQAFRK SIGIKIKEET ELIEGEVVEI QIDRSITGGH KQGKLTIKTT DMETIYELGN K MIDGLTKE KVLAGDVISI DKASGKITKL GRSFARSRDY DAMGADTRFV QCPEGELQKR KTVVHTVSLH EIDVINSRTQ GF LALFTGD TGEIRSEVRD QINTKVAEWK EEGKAEIVPG VLFIDEVHML DIECFSFINR ALEDEFAPIV MMATNRGVSK TRG TNYKSP HGLPLDLLDR SIIITTKSYN EQEIKTILSI RAQEEEVELS SDALDLLTKT GVETSLRYSS NLISVAQQIA MKRK NNTVE VEDVKRAYLL FLDSARSVKY VQENESQYID DQGNVQISIA K UniProtKB: RuvB-like protein 2 |
-Macromolecule #6: Ino eighty subunit 2
Macromolecule | Name: Ino eighty subunit 2 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c |
Molecular weight | Theoretical: 3.531075 KDa |
Sequence | String: FVKPRRPYNS EGMTRILRRY EEDLFCTF UniProtKB: Ino eighty subunit 2 |
-Macromolecule #7: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 6 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ChemComp-ADP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | cell |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: OTHER |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 43.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: -2.0 µm / Nominal defocus min: -1.0 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.48 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 22054 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |