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- EMDB-41110: Automethylated PRC2 dimer bound to nucleosome -

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Basic information

Entry
Database: EMDB / ID: EMD-41110
TitleAutomethylated PRC2 dimer bound to nucleosome
Map dataAutomethylated PRC2 dimer bound to nucleosome 3DFlex reconstruction locally filtered
Sample
  • Complex: Automethylated PRC2 dimer bound to nucleosome
    • Complex: Nucleosome
      • Protein or peptide: x 4 types
      • DNA: x 2 types
    • Complex: Proximal PRC2
      • Protein or peptide: x 6 types
    • Complex: Distal PRC2
  • Ligand: x 1 types
KeywordsHistone methyl transferase / gene repression / epigenetics / chromatin / GENE REGULATION
Function / homology
Function and homology information


hepatocyte homeostasis / regulation of kidney development / cellular response to trichostatin A / regulation of gliogenesis / negative regulation of striated muscle cell differentiation / [histone H3]-lysine27 N-trimethyltransferase / sex chromatin / negative regulation of keratinocyte differentiation / CAF-1 complex / histone H3K27 trimethyltransferase activity ...hepatocyte homeostasis / regulation of kidney development / cellular response to trichostatin A / regulation of gliogenesis / negative regulation of striated muscle cell differentiation / [histone H3]-lysine27 N-trimethyltransferase / sex chromatin / negative regulation of keratinocyte differentiation / CAF-1 complex / histone H3K27 trimethyltransferase activity / negative regulation of retinoic acid receptor signaling pathway / response to tetrachloromethane / cerebellar cortex development / random inactivation of X chromosome / primary miRNA binding / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration / regulatory ncRNA-mediated heterochromatin formation / histone H3K27 methyltransferase activity / facultative heterochromatin formation / positive regulation of cell cycle G1/S phase transition / NURF complex / NuRD complex / regulation of cell fate specification / negative regulation of stem cell population maintenance / DNA replication-dependent chromatin assembly / ESC/E(Z) complex / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / chromatin silencing complex / regulation of stem cell differentiation / protein-lysine N-methyltransferase activity / RSC-type complex / negative regulation of stem cell differentiation / Transcription of E2F targets under negative control by DREAM complex / pronucleus / cardiac muscle hypertrophy in response to stress / Polo-like kinase mediated events / synaptic transmission, GABAergic / positive regulation of dendrite development / histone H3 methyltransferase activity / lncRNA binding / negative regulation of G1/S transition of mitotic cell cycle / spinal cord development / G1 to G0 transition / negative regulation of gene expression, epigenetic / G1/S-Specific Transcription / positive regulation of stem cell population maintenance / ATPase complex / histone methyltransferase activity / Sin3-type complex / negative regulation of transcription elongation by RNA polymerase II / Transcriptional Regulation by E2F6 / oligodendrocyte differentiation / RNA Polymerase I Transcription Initiation / histone deacetylase complex / negative regulation of cell differentiation / G0 and Early G1 / subtelomeric heterochromatin formation / negative regulation of cytokine production involved in inflammatory response / RNA polymerase II core promoter sequence-specific DNA binding / ribonucleoprotein complex binding / pericentric heterochromatin / Cyclin E associated events during G1/S transition / Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 / positive regulation of epithelial to mesenchymal transition / Cyclin A:Cdk2-associated events at S phase entry / keratinocyte differentiation / Deposition of new CENPA-containing nucleosomes at the centromere / Regulation of TP53 Activity through Acetylation / protein localization to chromatin / enzyme activator activity / methylated histone binding / SUMOylation of chromatin organization proteins / B cell differentiation / positive regulation of GTPase activity / transcription corepressor binding / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / negative regulation of cell migration / PRC2 methylates histones and DNA / Regulation of PTEN gene transcription / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / stem cell differentiation / promoter-specific chromatin binding / hippocampus development / liver regeneration / transcription coregulator activity / negative regulation of transforming growth factor beta receptor signaling pathway / positive regulation of MAP kinase activity / positive regulation of protein serine/threonine kinase activity / brain development / protein modification process / regulation of circadian rhythm / chromatin DNA binding / heterochromatin formation / PKMTs methylate histone lysines / histone deacetylase binding / cellular response to hydrogen peroxide / Activation of anterior HOX genes in hindbrain development during early embryogenesis
Similarity search - Function
: / EZH2, SET domain / Polycomb protein, VEFS-Box / VEFS-Box of polycomb protein / Histone-lysine N-methyltransferase EZH1/EZH2 / Polycomb repressive complex 2 subunit EZH1/EZH2, tri-helical domain / Pre-SET CXC domain / : / WD repeat binding protein EZH2 / Polycomb repressive complex 2 tri-helical domain ...: / EZH2, SET domain / Polycomb protein, VEFS-Box / VEFS-Box of polycomb protein / Histone-lysine N-methyltransferase EZH1/EZH2 / Polycomb repressive complex 2 subunit EZH1/EZH2, tri-helical domain / Pre-SET CXC domain / : / WD repeat binding protein EZH2 / Polycomb repressive complex 2 tri-helical domain / CXC domain / Ezh2, MCSS domain / Tesmin/TSO1-like CXC domain / Tesmin/TSO1-like CXC domain / CXC domain / Histone-lysine N-methyltransferase EZH1/2-like / CXC domain profile. / Histone-binding protein RBBP4, N-terminal / Histone-binding protein RBBP4 or subunit C of CAF1 complex / : / : / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / SET domain / SET domain superfamily / SET domain profile. / SET domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / zinc finger / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily / Zinc finger C2H2 type domain signature. / Zinc finger C2H2-type / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H2A / Histone 2A / Histone H4, conserved site / Histone H4 signature. / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Polycomb protein EED / Histone H2B 1.1 / Histone H2A type 1 / Histone H4 / Histone H3.2 / Histone-binding protein RBBP4 / Polycomb protein SUZ12 / Histone-lysine N-methyltransferase EZH2 / Zinc finger protein AEBP2
Similarity search - Component
Biological speciesHomo sapiens (human) / Xenopus laevis (African clawed frog) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.2 Å
AuthorsSauer PV / Pavlenko E / Nogales E / Poepsel S
Funding support United States, 1 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Mol Cell / Year: 2024
Title: Activation of automethylated PRC2 by dimerization on chromatin.
Authors: Paul V Sauer / Egor Pavlenko / Trinity Cookis / Linda C Zirden / Juliane Renn / Ankush Singhal / Pascal Hunold / Michaela N Hoehne-Wiechmann / Olivia van Ray / Farnusch Kaschani / Markus ...Authors: Paul V Sauer / Egor Pavlenko / Trinity Cookis / Linda C Zirden / Juliane Renn / Ankush Singhal / Pascal Hunold / Michaela N Hoehne-Wiechmann / Olivia van Ray / Farnusch Kaschani / Markus Kaiser / Robert Hänsel-Hertsch / Karissa Y Sanbonmatsu / Eva Nogales / Simon Poepsel /
Abstract: Polycomb repressive complex 2 (PRC2) is an epigenetic regulator that trimethylates lysine 27 of histone 3 (H3K27me3) and is essential for embryonic development and cellular differentiation. H3K27me3 ...Polycomb repressive complex 2 (PRC2) is an epigenetic regulator that trimethylates lysine 27 of histone 3 (H3K27me3) and is essential for embryonic development and cellular differentiation. H3K27me3 is associated with transcriptionally repressed chromatin and is established when PRC2 is allosterically activated upon methyl-lysine binding by the regulatory subunit EED. Automethylation of the catalytic subunit enhancer of zeste homolog 2 (EZH2) stimulates its activity by an unknown mechanism. Here, we show that human PRC2 forms a dimer on chromatin in which an inactive, automethylated PRC2 protomer is the allosteric activator of a second PRC2 that is poised to methylate H3 of a substrate nucleosome. Functional assays support our model of allosteric trans-autoactivation via EED, suggesting a previously unknown mechanism mediating context-dependent activation of PRC2. Our work showcases the molecular mechanism of auto-modification-coupled dimerization in the regulation of chromatin-modifying complexes.
History
DepositionJun 23, 2023-
Header (metadata) releaseSep 25, 2024-
Map releaseSep 25, 2024-
UpdateNov 6, 2024-
Current statusNov 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_41110.png

Downloads & links

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Map

FileDownload / File: emd_41110.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationAutomethylated PRC2 dimer bound to nucleosome 3DFlex reconstruction locally filtered
Projections & slices

Image control

Size
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.3 Å/pix.
x 200 pix.
= 460. Å		2.3 Å/pix.
x 200 pix.
= 460. Å		2.3 Å/pix.
x 200 pix.
= 460. Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 2.3 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.02
Minimum - Maximum-0.07561512 - 0.1978516
Average (Standard dev.)0.00049658597 (±0.004686018)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 460.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_41110_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Automethylated PRC2 dimer bound to nucleosome

EntireName: Automethylated PRC2 dimer bound to nucleosome
Components
  • Complex: Automethylated PRC2 dimer bound to nucleosome
    • Complex: Nucleosome
      • Protein or peptide: Histone H3.2
      • DNA: DNA (226-MER)
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1
      • Protein or peptide: Histone H2B 1.1
      • DNA: DNA (226-MER)
    • Complex: Proximal PRC2
      • Protein or peptide: Polycomb protein SUZ12
      • Protein or peptide: Histone-lysine N-methyltransferase EZH2
      • Protein or peptide: Polycomb protein EED
      • Protein or peptide: Histone-binding protein RBBP4
      • Protein or peptide: Zinc finger protein AEBP2
      • Protein or peptide: activating methylated peptide
    • Complex: Distal PRC2
  • Ligand: S-ADENOSYL-L-HOMOCYSTEINE

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Supramolecule #1: Automethylated PRC2 dimer bound to nucleosome

SupramoleculeName: Automethylated PRC2 dimer bound to nucleosome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#12
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 290 KDa

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Supramolecule #2: Nucleosome

SupramoleculeName: Nucleosome / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #6-#11
Source (natural)Organism: Xenopus laevis (African clawed frog)

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Supramolecule #3: Proximal PRC2

SupramoleculeName: Proximal PRC2 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1-#5, #12
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: Distal PRC2

SupramoleculeName: Distal PRC2 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Polycomb protein SUZ12

MacromoleculeName: Polycomb protein SUZ12 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 72.266359 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MVLPVKKPKM EHVQADHELF LQAFEKPTQI YRFLRTRNLI APIFLHRTLT YMSHRNSRTN IKRKTFKVDD MLSKVEKMKG EQESHSLSA HLQLTFTGFF HKNDKPSPNS ENEQNSVTLE VLLVKVCHKK RKDVSCPIRQ VPTGKKQVPL NPDLNQTKPG N FPSLAVSS ...String:
MVLPVKKPKM EHVQADHELF LQAFEKPTQI YRFLRTRNLI APIFLHRTLT YMSHRNSRTN IKRKTFKVDD MLSKVEKMKG EQESHSLSA HLQLTFTGFF HKNDKPSPNS ENEQNSVTLE VLLVKVCHKK RKDVSCPIRQ VPTGKKQVPL NPDLNQTKPG N FPSLAVSS NEFEPSNSHM VKSYSLLFRV TRPGRREFNG MINGETNENI DVNEELPARR KRNREDGEKT FVAQMTVFDK NR RLQLLDG EYEVAMQEME ECPISKKRAT WETILDGKRL PPFETFSQGP TLQFTLRWTG ETNDKSTAPI AKPLATRNSE SLH QENKPG SVKPTQTIAV KESLTTDLQT RKEKDTPNEN RQKLRIFYQF LYNNNTRQQT EARDDLHCPW CTLNCRKLYS LLKH LKLCH SRFIFNYVYH PKGARIDVSI NECYDGSYAG NPQDIHRQPG FAFSRNGPVK RTPITHILVC RPKRTKASMS EFLES EDGE VEQQRTYSSG HNRLYFHSDT CLPLRPQEME VDSEDEKDPE WLREKTITQI EEFSDVNEGE KEVMKLWNLH VMKHGF IAD NQMNHACMLF VENYGQKIIK KNLCRNFMLH LVSMHDFNLI SIMSIDKAVT KLREMQ

UniProtKB: Polycomb protein SUZ12

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Macromolecule #2: Histone-lysine N-methyltransferase EZH2

MacromoleculeName: Histone-lysine N-methyltransferase EZH2 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: [histone H3]-lysine27 N-trimethyltransferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 86.174984 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNAGQTGKKS EKGPVACRKR VKSEYMRLRQ LKRFRRADEV KSMFSSNRQK ILERTEILNQ EWKQRRIQPV HILTSVSSLR GTRECSVTS DLDFPTQVIP LKTLNAVASV PIMYSWSPLQ QNFMVEDETV LHNIPYMGDE VLDQDGTFIE ELIKNYDGKV H GDRECGFI ...String:
SNAGQTGKKS EKGPVACRKR VKSEYMRLRQ LKRFRRADEV KSMFSSNRQK ILERTEILNQ EWKQRRIQPV HILTSVSSLR GTRECSVTS DLDFPTQVIP LKTLNAVASV PIMYSWSPLQ QNFMVEDETV LHNIPYMGDE VLDQDGTFIE ELIKNYDGKV H GDRECGFI NDEIFVELVN ALGQYNDDDD DDDGDDPEER EEKQKDLEDH RDDKESRPPR KFPSDKIFEA ISSMFPDKGT AE ELKEKYK ELTEQQLPGA LPPECTPNID GPNAKSVQRE QSLHSFHTLF CRRCFKYDCF LHRKCNYSFH ATPNTYKRKN TET ALDNKP CGPQCYQHLE GAKEFAAALT AERIKTPPKR PGGRRRGRLP NNSSRPSTPT INVLESKDTD SDREAGTETG GENN DKEEE EKKDETSSSS EANSRCQTPI KMKPNIEPPE NVEWSGAEAS MFRVLIGTYY DNFCAIARLI GTKTCRQVYE FRVKE SSII APAPAEDVDT PPRKKKRKHR LWAAHCRKIQ LKKDGSSNHV YNYQPCDHPR QPCDSSCPCV IAQNFCEKFC QCSSEC QNR FPGCRCKAQC NTKQCPCYLA VRECDPDLCL TCGAADHWDS KNVSCKNCSI QRGSKKHLLL APSDVAGWGI FIKDPVQ KN EFISEYCGEI ISQDEADRRG KVYDKYMCSF LFNLNNDFVV DATRKGNKIR FANHSVNPNC YAKVMMVNGD HRIGIFAK R AIQTGEELFF DYRYSQADAL KYVGIEREME IP

UniProtKB: Histone-lysine N-methyltransferase EZH2

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Macromolecule #3: Polycomb protein EED

MacromoleculeName: Polycomb protein EED / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 50.267691 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSEREVSTAP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT ERPDTPTNTP NAPGRKSWGK GKWKSKKCKY SFKCVNSLK EDHNQPLFGV QFNWHSKEGD PLVFATVGSN RVTLYECHSQ GEIRLLQSYV DADADENFYT CAWTYDSNTS H PLLAVAGS ...String:
MSEREVSTAP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT ERPDTPTNTP NAPGRKSWGK GKWKSKKCKY SFKCVNSLK EDHNQPLFGV QFNWHSKEGD PLVFATVGSN RVTLYECHSQ GEIRLLQSYV DADADENFYT CAWTYDSNTS H PLLAVAGS RGIIRIINPI TMQCIKHYVG HGNAINELKF HPRDPNLLLS VSKDHALRLW NIQTDTLVAI FGGVEGHRDE VL SADYDLL GEKIMSCGMD HSLKLWRINS KRMMNAIKES YDYNPNKTNR PFISQKIHFP DFSTRDIHRN YVDCVRWLGD LIL SKSCEN AIVCWKPGKM EDDIDKIKPS ESNVTILGRF DYSQCDIWYM RFSMDFWQKM LALGNQVGKL YVWDLEVEDP HKAK CTTLT HHKCGAAIRQ TSFSRDSSIL IAVCDDASIW RWDRLR

UniProtKB: Polycomb protein EED

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Macromolecule #4: Histone-binding protein RBBP4

MacromoleculeName: Histone-binding protein RBBP4 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 47.709527 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD FSIHRLVLGT HTSDEQNHLV IASVQLPND DAQFDASHYD SEKGEFGGFG SVSGKIEIEI KINHEGEVNR ARYMPQNPCI IATKTPSSDV LVFDYTKHPS K PDPSGECN ...String:
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD FSIHRLVLGT HTSDEQNHLV IASVQLPND DAQFDASHYD SEKGEFGGFG SVSGKIEIEI KINHEGEVNR ARYMPQNPCI IATKTPSSDV LVFDYTKHPS K PDPSGECN PDLRLRGHQK EGYGLSWNPN LSGHLLSASD DHTICLWDIS AVPKEGKVVD AKTIFTGHTA VVEDVSWHLL HE SLFGSVA DDQKLMIWDT RSNNTSKPSH SVDAHTAEVN CLSFNPYSEF ILATGSADKT VALWDLRNLK LKLHSFESHK DEI FQVQWS PHNETILASS GTDRRLNVWD LSKIGEEQSP EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWVICSVSED NIMQ VWQMA ENIYNDEDPE GSVDPEGQGS

UniProtKB: Histone-binding protein RBBP4

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Macromolecule #5: Zinc finger protein AEBP2

MacromoleculeName: Zinc finger protein AEBP2 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.183195 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNAYTRRYSS ISSTIMDVDS TISSGRSTPA MMNGQGSTTS SSKNIAYNCC WDQCQACFNS SPDLADHIRS IHVDGQRGGV FVCLWKGCK VYNTPSTSQS WLQRHMLTHS GDKPFKCVVG GCNASFASQG GLARHVPTHF SQQNSSKVSS QPKAKEESPS K AGMNKRRK ...String:
SNAYTRRYSS ISSTIMDVDS TISSGRSTPA MMNGQGSTTS SSKNIAYNCC WDQCQACFNS SPDLADHIRS IHVDGQRGGV FVCLWKGCK VYNTPSTSQS WLQRHMLTHS GDKPFKCVVG GCNASFASQG GLARHVPTHF SQQNSSKVSS QPKAKEESPS K AGMNKRRK LKNKRRRSLP RPHDFFDAQT LDAIRHRAIC FNLSAHIESL GKGHSVVFHS TVIAKRKEDS GKIKLLLHWM PE DILPDVW VNESERHQLK TKVVHLSKLP KDTALLLDPN IYRTMPQKRL KRTLIRKVFN LYLSKQ

UniProtKB: Zinc finger protein AEBP2

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Macromolecule #6: Histone H3.2

MacromoleculeName: Histone H3.2 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 15.435126 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEASEA YLVALFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.2

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Macromolecule #8: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 11.625634 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGGSSG

UniProtKB: Histone H4

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Macromolecule #9: Histone H2A type 1

MacromoleculeName: Histone H2A type 1 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 14.355659 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SNAMSGRGKQ GGKTRAKAKT RSSRAGLQFP VGRVHRLLRK GNYAERVGAG APVYLAAVLE YLTAEILELA GNAARDNKKT RIIPRHLQL AVRNDEELNK LLGRVTIAQG GVLPNIQSVL LPKCTESSKS AKSK

UniProtKB: Histone H2A type 1

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Macromolecule #10: Histone H2B 1.1

MacromoleculeName: Histone H2B 1.1 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 13.655948 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MAKSAPAPKK GSKKAVTKTQ KKDGKKRRKT RKESYAIYVY KVLKQVHPDT GISSKAMSIM NSFVNDVFER IAGEASRLAH YNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY TSAK

UniProtKB: Histone H2B 1.1

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Macromolecule #12: activating methylated peptide

MacromoleculeName: activating methylated peptide / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.125428 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(M3L)(UNK) (UNK)(UNK)

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Macromolecule #7: DNA (226-MER)

MacromoleculeName: DNA (226-MER) / type: dna / ID: 7 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 66.53932 KDa
SequenceString: (DA)(DT)(DC)(DG)(DG)(DG)(DA)(DG)(DC)(DT) (DC)(DC)(DG)(DA)(DC)(DC)(DG)(DA)(DA)(DT) (DG)(DA)(DC)(DA)(DT)(DG)(DC)(DA)(DT) (DG)(DC)(DA)(DT)(DA)(DC)(DA)(DG)(DG)(DA) (DT) (DG)(DT)(DA)(DT)(DA)(DT) ...String:
(DA)(DT)(DC)(DG)(DG)(DG)(DA)(DG)(DC)(DT) (DC)(DC)(DG)(DA)(DC)(DC)(DG)(DA)(DA)(DT) (DG)(DA)(DC)(DA)(DT)(DG)(DC)(DA)(DT) (DG)(DC)(DA)(DT)(DA)(DC)(DA)(DG)(DG)(DA) (DT) (DG)(DT)(DA)(DT)(DA)(DT)(DA)(DC) (DC)(DT)(DG)(DA)(DC)(DA)(DC)(DG)(DT)(DG) (DC)(DC) (DT)(DG)(DG)(DA)(DG)(DA)(DC) (DT)(DA)(DG)(DG)(DG)(DA)(DG)(DT)(DA)(DA) (DC)(DC)(DC) (DC)(DC)(DT)(DT)(DG)(DG) (DC)(DG)(DG)(DT)(DT)(DA)(DA)(DA)(DA)(DC) (DG)(DC)(DG)(DG) (DG)(DG)(DG)(DA)(DC) (DA)(DG)(DC)(DG)(DC)(DG)(DT)(DA)(DC)(DG) (DT)(DG)(DC)(DG)(DT) (DT)(DT)(DA)(DA) (DG)(DC)(DG)(DG)(DT)(DG)(DC)(DT)(DA)(DG) (DA)(DG)(DC)(DT)(DG)(DC) (DC)(DT)(DA) (DC)(DG)(DA)(DC)(DC)(DA)(DA)(DT)(DG)(DG) (DA)(DG)(DC)(DG)(DG)(DC)(DC) (DT)(DC) (DG)(DG)(DC)(DA)(DC)(DC)(DG)(DG)(DG)(DA) (DT)(DC)(DC)(DC)(DC)(DC)(DA)(DG) (DC) (DC)(DG)(DC)(DC)(DG)(DG)(DC)(DA)(DG)(DC) (DG)(DC)(DA)(DG)(DC)(DG)(DC)(DC)(DT) (DG)(DA)(DC)(DG)(DG)(DG)(DC)(DA)(DC)(DA) (DC)(DA)(DG)(DT)(DC)

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Macromolecule #11: DNA (226-MER)

MacromoleculeName: DNA (226-MER) / type: dna / ID: 11 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 65.905852 KDa
SequenceString: (DG)(DA)(DC)(DT)(DG)(DT)(DG)(DT)(DG)(DC) (DC)(DC)(DG)(DT)(DC)(DA)(DG)(DA)(DC)(DG) (DC)(DT)(DG)(DC)(DG)(DC)(DC)(DG)(DC) (DC)(DG)(DG)(DC)(DG)(DG)(DC)(DC)(DG)(DG) (DA) (DG)(DA)(DA)(DT)(DC)(DC) ...String:
(DG)(DA)(DC)(DT)(DG)(DT)(DG)(DT)(DG)(DC) (DC)(DC)(DG)(DT)(DC)(DA)(DG)(DA)(DC)(DG) (DC)(DT)(DG)(DC)(DG)(DC)(DC)(DG)(DC) (DC)(DG)(DG)(DC)(DG)(DG)(DC)(DC)(DG)(DG) (DA) (DG)(DA)(DA)(DT)(DC)(DC)(DC)(DG) (DG)(DT)(DG)(DC)(DC)(DG)(DA)(DG)(DG)(DC) (DC)(DG) (DC)(DC)(DC)(DT)(DA)(DT)(DT) (DG)(DG)(DT)(DC)(DG)(DT)(DA)(DG)(DA)(DC) (DA)(DG)(DC) (DC)(DC)(DC)(DA)(DG)(DC) (DA)(DC)(DC)(DG)(DC)(DC)(DT)(DA)(DA)(DA) (DC)(DG)(DC)(DA) (DC)(DG)(DT)(DA)(DC) (DG)(DC)(DG)(DC)(DC)(DG)(DT)(DC)(DC)(DC) (DC)(DC)(DG)(DC)(DG) (DT)(DT)(DT)(DT) (DA)(DA)(DC)(DC)(DG)(DC)(DC)(DA)(DA)(DG) (DG)(DG)(DG)(DA)(DT)(DT) (DA)(DC)(DC) (DC)(DC)(DC)(DC)(DA)(DG)(DT)(DC)(DC)(DC) (DC)(DA)(DG)(DG)(DC)(DA)(DC) (DG)(DT) (DG)(DC)(DC)(DA)(DG)(DA)(DT)(DA)(DT)(DA) (DT)(DA)(DC)(DA)(DT)(DC)(DC)(DC) (DG) (DT)(DA)(DC)(DG)(DC)(DA)(DC)(DG)(DC)(DA) (DC)(DA)(DT)(DC)(DA)(DT)(DT)(DC)(DG) (DA)(DT)(DC)(DG)(DG)(DA)(DG)(DC)(DT)(DC) (DC)(DC)(DG)(DA)(DT)

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Macromolecule #13: S-ADENOSYL-L-HOMOCYSTEINE

MacromoleculeName: S-ADENOSYL-L-HOMOCYSTEINE / type: ligand / ID: 13 / Number of copies: 2 / Formula: SAH
Molecular weightTheoretical: 384.411 Da
Chemical component information

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.8
GridMaterial: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Details: Streptavidin affinity grid
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

7334

Final reconstructionResolution.type: BY AUTHOR / Resolution: 6.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 34000
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-8t9g:
Automethylated PRC2 dimer bound to nucleosome

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