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- EMDB-28599: Class2 of the INO80-Hexasome complex -

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Basic information

Entry
Database: EMDB / ID: EMD-28599
TitleClass2 of the INO80-Hexasome complex
Map dataClass2,INO80-Hex,overall
Sample
  • Complex: INO80-Hex
    • Protein or peptide: Chromatin-remodeling ATPase INO80
    • Protein or peptide: Actin-related protein 5
    • Protein or peptide: Chromatin-remodeling complex subunit IES6
    • Protein or peptide: Ino eighty subunit 2
  • Protein or peptide: RuvB-like protein 1
  • Protein or peptide: RuvB-like protein 2
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
KeywordsChromatin Remodeler / hexasome / DNA BINDING PROTEIN
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 / ATP-dependent chromatin remodeler activity / DNA duplex unwinding / 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 / ATP-dependent chromatin remodeler activity / DNA duplex unwinding / 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
DBINO domain / DNA helicase Ino80 / DNA-binding domain / DBINO domain profile. / INO80 complex subunit B-like conserved region / INO80 complex, subunit Ies2 / INO80 complex, subunit Ies6 / PAPA-1-like conserved region / PAPA-1 / : ...DBINO domain / DNA helicase Ino80 / DNA-binding domain / DBINO domain profile. / INO80 complex subunit B-like conserved region / INO80 complex, subunit Ies2 / INO80 complex, subunit Ies6 / PAPA-1-like conserved region / PAPA-1 / : / Vps72/YL1, C-terminal / YL1 nuclear protein C-terminal domain / YL1 nuclear protein C-terminal domain / RuvB-like / RuvB-like, AAA-lid domain / RuvBL1/2, DNA/RNA binding domain / TIP49 P-loop domain / TIP49 AAA-lid domain / TIP49, P-loop domain / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / Actin / Actin family / Actin / Helicase conserved C-terminal domain / ATPase, nucleotide binding domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Chromatin-remodeling complex subunit IES6 / Ino eighty subunit 2 / Chromatin-remodeling ATPase INO80 / Actin-related protein 5 / RuvB-like protein 1 / RuvB-like protein 2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Saccharomyces cerevisiae S288C (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsWu H / Munoz E / Gourdet M / Cheng YF / Narlikar G
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD) United States
CitationJournal: 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
DepositionOct 17, 2022-
Header (metadata) releaseJul 19, 2023-
Map releaseJul 19, 2023-
UpdateJun 19, 2024-
Current statusJun 19, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_28599.png

Downloads & links

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Map

FileDownload / File: emd_28599.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationClass2,INO80-Hex,overall
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 480 pix.
= 400.8 Å		0.84 Å/pix.
x 480 pix.
= 400.8 Å		0.84 Å/pix.
x 480 pix.
= 400.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.835 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.06
Minimum - Maximum-0.03348417 - 1.5980135
Average (Standard dev.)0.0010057389 (±0.020413417)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 400.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Class2, INO80-Hex,hex

Fileemd_28599_additional_1.map
AnnotationClass2, INO80-Hex,hex
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Class2,INO80-Hex,overall, half1

Fileemd_28599_half_map_1.map
AnnotationClass2,INO80-Hex,overall, half1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Class2,INO80-Hex,overall, half2

Fileemd_28599_half_map_2.map
AnnotationClass2,INO80-Hex,overall, half2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : INO80-Hex

EntireName: INO80-Hex
Components
  • Complex: INO80-Hex
    • Protein or peptide: Chromatin-remodeling ATPase INO80
    • Protein or peptide: Actin-related protein 5
    • Protein or peptide: Chromatin-remodeling complex subunit IES6
    • Protein or peptide: Ino eighty subunit 2
  • Protein or peptide: RuvB-like protein 1
  • Protein or peptide: RuvB-like protein 2
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: INO80-Hex

SupramoleculeName: INO80-Hex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #5, #1-#2, #6
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Macromolecule #1: Actin-related protein 5

MacromoleculeName: Actin-related protein 5 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 86.522047 KDa
SequenceString: KAVVIDDPPL RQTPEPFDEQ SAYNPQSPIA IDFGSSKLRA GFVNHATPTH IFPNALTKFR DRKLNKNFTF VGNDTLLDQA VRSQSRSPF DGPFVTNWNL TEEILDYTFH HLGVVPDNGI PNPILLTERL ATVQSQRTNW YQILFETYNV PGVTFGIDSL F SFYNYNPS ...String:
KAVVIDDPPL RQTPEPFDEQ SAYNPQSPIA IDFGSSKLRA GFVNHATPTH IFPNALTKFR DRKLNKNFTF VGNDTLLDQA VRSQSRSPF DGPFVTNWNL TEEILDYTFH HLGVVPDNGI PNPILLTERL ATVQSQRTNW YQILFETYNV PGVTFGIDSL F SFYNYNPS GNKTGLVISC GHEDTNVIPV VDGAGILTDA KRINWGGHQA VDYLNDLMAL KYPYFPTKMS YLQYETMYKD YC YVSRNYD EDIEKILTLE NLDTNDVVVE APFTEVLQPQ KTEEELRIQA EKRKETGKRL QEQARLKRME KLVQKQEEFE YFS KVRDQL IDEPKKKVLS VLQNAGFDDE RDFKKYLHSL EQSLKKAQMV EAEDDSHLDE MNEDKTAQKF DLLDIADEDL NEDQ IKEKR KQRFLKASQD ARQKAKEEKE RVAKEEEEKK LKEQQWRETD LNGWIKDKRL KLNKLIKRRK EKLKLRDEMK DRKSQ VSQN RMKNLASLAE DNVKQGAKRN RHQATIDNDP NDTFGANDED WLIYTDITQN PEAFEEALEY EYKDIVELER LLLEHD PNF TEEDTLEAQY DWRNSILHLF LRGPRPHDSE NIHEQHQMHL NVERIRVPEV IFQPTMGGQD QAGICELSET ILLKKFG SQ PGKLSQTSID MVNNVLITGG NAKVPGLKER IVKEFTGFLP TGTNITVNMS SDPSLDAWKG MAALARNEEQ YRKTVISK K EYEEYGPEYI KEHKLGNTKY FED

UniProtKB: Actin-related protein 5

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Macromolecule #2: Chromatin-remodeling complex subunit IES6

MacromoleculeName: Chromatin-remodeling complex subunit IES6 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 15.881406 KDa
SequenceString:
ERLLFLRSVG ERNEIGFPSR FKSAHYKKPT RRHKSARQLI SDENKRINAL LTKANKAAES STAARRLVPK ATYFSVEAPP SIRPAKKYC DVTGLKGFYK SPTNNIRYHN AEIYQLIVKP MAPGVDQEYL KLRGANFVLK

UniProtKB: Chromatin-remodeling complex subunit IES6

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Macromolecule #3: RuvB-like protein 1

MacromoleculeName: RuvB-like protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 48.543805 KDa
SequenceString: 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

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Macromolecule #4: RuvB-like protein 2

MacromoleculeName: RuvB-like protein 2 / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 50.153898 KDa
SequenceString: 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 KSADPDAMDT TE

UniProtKB: RuvB-like protein 2

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Macromolecule #5: Chromatin-remodeling ATPase INO80

MacromoleculeName: Chromatin-remodeling ATPase INO80 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 54.985918 KDa
SequenceString: 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 M

UniProtKB: Chromatin-remodeling ATPase INO80

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Macromolecule #6: Ino eighty subunit 2

MacromoleculeName: Ino eighty subunit 2 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 3.531075 KDa
SequenceString:
FVKPRRPYNS EGMTRILRRY EEDLFCTF

UniProtKB: Ino eighty subunit 2

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Macromolecule #7: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 6 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statecell

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: OTHER

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 67.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination 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

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 130147
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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