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- EMDB-18581: Human Tip60 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-18581
TitleHuman Tip60 complex
Map dataOverall structure
Sample
  • Cell: Tip60 complex
    • Protein or peptide: EP400
    • Protein or peptide: EPC1
    • Protein or peptide: VPS72
    • Protein or peptide: DMAP1
    • Protein or peptide: ACL6A
    • Protein or peptide: ACTIN
    • Protein or peptide: RUVBL1
    • Protein or peptide: RUVBL2
KeywordsEukaryotic transcription / Histone acetyltransferase / chromatin remodeling / Complex / TRANSCRIPTION
Function / homology
Function and homology information


piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / telomerase RNA localization to Cajal body / positive regulation of norepinephrine uptake / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / sperm DNA condensation / histone chaperone activity / establishment of protein localization to chromatin / cellular response to cytochalasin B ...piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / telomerase RNA localization to Cajal body / positive regulation of norepinephrine uptake / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / sperm DNA condensation / histone chaperone activity / establishment of protein localization to chromatin / cellular response to cytochalasin B / R2TP complex / bBAF complex / npBAF complex / regulation of transepithelial transport / nBAF complex / brahma complex / dynein axonemal particle / morphogenesis of a polarized epithelium / neural retina development / protein localization to adherens junction / postsynaptic actin cytoskeleton / Swr1 complex / structural constituent of postsynaptic actin cytoskeleton / protein antigen binding / Formation of the dystrophin-glycoprotein complex (DGC) / GBAF complex / Formation of annular gap junctions / Tat protein binding / Gap junction degradation / regulation of G0 to G1 transition / Folding of actin by CCT/TriC / Cell-extracellular matrix interactions / dense body / RPAP3/R2TP/prefoldin-like complex / chromatin-protein adaptor activity / Ino80 complex / regulation of nucleotide-excision repair / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / apical protein localization / regulation of double-strand break repair / blastocyst formation / box C/D snoRNP assembly / adherens junction assembly / RHOF GTPase cycle / Adherens junctions interactions / tight junction / Sensory processing of sound by outer hair cells of the cochlea / protein folding chaperone complex / Interaction between L1 and Ankyrins / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / Sensory processing of sound by inner hair cells of the cochlea / positive regulation of T cell differentiation / regulation of norepinephrine uptake / transporter regulator activity / apical junction complex / nitric-oxide synthase binding / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / positive regulation of double-strand break repair / spinal cord development / maintenance of blood-brain barrier / regulation of chromosome organization / NuA4 histone acetyltransferase complex / negative regulation of gene expression, epigenetic / establishment or maintenance of cell polarity / cortical cytoskeleton / spermatid development / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of stem cell population maintenance / Transcriptional Regulation by E2F6 / Regulation of MITF-M-dependent genes involved in pigmentation / Recycling pathway of L1 / regulation of synaptic vesicle endocytosis / regulation of G1/S transition of mitotic cell cycle / regulation of DNA replication / TFIID-class transcription factor complex binding / brush border / regulation of embryonic development / kinesin binding / MLL1 complex / somatic stem cell population maintenance / Telomere Extension By Telomerase / EPH-ephrin mediated repulsion of cells / negative regulation of cell differentiation / RHO GTPases Activate WASPs and WAVEs / enzyme-substrate adaptor activity / positive regulation of myoblast differentiation / RHO GTPases activate IQGAPs / positive regulation of double-strand break repair via homologous recombination / regulation of DNA repair / regulation of protein localization to plasma membrane / RNA polymerase II core promoter sequence-specific DNA binding / DNA helicase activity / cytoskeleton organization / Deposition of new CENPA-containing nucleosomes at the centromere / EPHB-mediated forward signaling / TBP-class protein binding / substantia nigra development / calyx of Held
Similarity search - Function
Enhancer of polycomb, C-terminal / Enhancer of Polycomb C-terminus / DNA methyltransferase 1-associated 1 / DNA methyltransferase 1-associated protein 1 (DMAP1) / E1A-binding protein p400, N-terminal / E1A-binding protein p400, N-terminal / SWR1-complex protein 4/DNA methyltransferase 1-associated protein 1 / DAMP1, SANT/Myb-like domain / SANT/Myb-like domain of DAMP1 / Enhancer of polycomb protein ...Enhancer of polycomb, C-terminal / Enhancer of Polycomb C-terminus / DNA methyltransferase 1-associated 1 / DNA methyltransferase 1-associated protein 1 (DMAP1) / E1A-binding protein p400, N-terminal / E1A-binding protein p400, N-terminal / SWR1-complex protein 4/DNA methyltransferase 1-associated protein 1 / DAMP1, SANT/Myb-like domain / SANT/Myb-like domain of DAMP1 / Enhancer of polycomb protein / Vps72/YL1, N-terminal / YL1 nuclear protein / Vps72/YL1, C-terminal / YL1 nuclear protein C-terminal domain / YL1 nuclear protein C-terminal domain / Myb-like domain profile. / domain in helicases and associated with SANT domains / 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 / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / Enhancer of polycomb-like, N-terminal / Enhancer of polycomb-like / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / SANT/Myb domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / 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
Actin-like protein 6A / Actin, cytoplasmic 1 / Vacuolar protein sorting-associated protein 72 homolog / E1A-binding protein p400 / Enhancer of polycomb homolog 1 / DNA methyltransferase 1-associated protein 1 / RuvB-like 2 / RuvB-like 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.52 Å
AuthorsLi C / Smirnova E / Schnitzler C / Crucifix C / Concordet JP / Brion A / Poterszman A / Schultz P / Papai G / Ben-Shem A
Funding support France, 1 items
OrganizationGrant numberCountry
La ligue contre le cancer France
CitationJournal: Nature / Year: 2024
Title: Structure of the human TIP60-C histone exchange and acetyltransferase complex.
Authors: Changqing Li / Ekaterina Smirnova / Charlotte Schnitzler / Corinne Crucifix / Jean Paul Concordet / Alice Brion / Arnaud Poterszman / Patrick Schultz / Gabor Papai / Adam Ben-Shem /
Abstract: Chromatin structure is a key regulator of DNA transcription, replication and repair. In humans, the TIP60-EP400 complex (TIP60-C) is a 20-subunit assembly that affects chromatin structure through two ...Chromatin structure is a key regulator of DNA transcription, replication and repair. In humans, the TIP60-EP400 complex (TIP60-C) is a 20-subunit assembly that affects chromatin structure through two enzymatic activities: ATP-dependent exchange of histone H2A-H2B for H2A.Z-H2B, and histone acetylation. In yeast, however, these activities are performed by two independent complexes-SWR1 and NuA4, respectively. How the activities of the two complexes are merged into one supercomplex in humans, and what this association entails for the structure and mechanism of the proteins and their recruitment to chromatin, are unknown. Here we describe the structure of the endogenous human TIP60-C. We find a three-lobed architecture composed of SWR1-like (SWR1L) and NuA4-like (NuA4L) parts, which associate with a TRRAP activator-binding module. The huge EP400 subunit contains the ATPase motor, traverses the junction between SWR1L and NuA4L twice and constitutes the scaffold of the three-lobed architecture. NuA4L is completely rearranged compared with its yeast counterpart. TRRAP is flexibly tethered to NuA4L-in stark contrast to its robust connection to the completely opposite side of NuA4 in yeast. A modelled nucleosome bound to SWR1L, supported by tests of TIP60-C activity, suggests that some aspects of the histone exchange mechanism diverge from what is seen in yeast. Furthermore, a fixed actin module (as opposed to the mobile actin subcomplex in SWR1; ref. ), the flexibility of TRRAP and the weak effect of extranucleosomal DNA on exchange activity lead to a different, activator-based mode of enlisting TIP60-C to chromatin.
History
DepositionOct 3, 2023-
Header (metadata) releaseAug 7, 2024-
Map releaseAug 7, 2024-
UpdateDec 4, 2024-
Current statusDec 4, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18581.png

Downloads & links

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Map

FileDownload / File: emd_18581.map.gz / Format: CCP4 / Size: 1.2 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationOverall structure
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.73 Å/pix.
x 686 pix.
= 500.78 Å		0.73 Å/pix.
x 686 pix.
= 500.78 Å		0.73 Å/pix.
x 686 pix.
= 500.78 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.73 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.06
Minimum - Maximum-0.22599822 - 0.5981678
Average (Standard dev.)0.0008916346 (±0.008442004)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions686686686
Spacing686686686
CellA=B=C: 500.78 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_18581_msk_1.map
Projections & Slices
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Half map: Half map A

Fileemd_18581_half_map_1.map
AnnotationHalf map A
Projections & Slices
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Half map: Half map B

Fileemd_18581_half_map_2.map
AnnotationHalf map B
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Sample components

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Entire : Tip60 complex

EntireName: Tip60 complex
Components
  • Cell: Tip60 complex
    • Protein or peptide: EP400
    • Protein or peptide: EPC1
    • Protein or peptide: VPS72
    • Protein or peptide: DMAP1
    • Protein or peptide: ACL6A
    • Protein or peptide: ACTIN
    • Protein or peptide: RUVBL1
    • Protein or peptide: RUVBL2

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Supramolecule #1: Tip60 complex

SupramoleculeName: Tip60 complex / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human) / Strain: K562

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Macromolecule #1: EP400

MacromoleculeName: EP400 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ LMNRSPATG QNVNITLQSV GPVVGGNQQI TLAPLPLPSP TSPGFQFSAQ PRRFEHGSPS Y IQVTSPLS QQVQTQSPTQ PSPGPGQALQ NVRAGAPGPG LGLCSSSPTG ...String:
MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ LMNRSPATG QNVNITLQSV GPVVGGNQQI TLAPLPLPSP TSPGFQFSAQ PRRFEHGSPS Y IQVTSPLS QQVQTQSPTQ PSPGPGQALQ NVRAGAPGPG LGLCSSSPTG GFVDASVLVR QI SLSPSSG GHFVFQDGSG LTQIAQGAQV QLQHPGTPIT VRERRPSQPH TQSGGTIHHL GPQ SPAAAG GAGLQPLASP SHITTANLPP QISSIIQGQL VQQQQVLQGP PLPRPLGFER TPGV LLPGA GGAAGFGMTS PPPPTSPSRT AVPPGLSSLP LTSVGNTGMK KVPKKLEEIP PASPE MAQM RKQCLDYHYQ EMQALKEVFK EYLIELFFLQ HFQGNMMDFL AFKKKHYAPL QAYLRQ NDL DIEEEEEEEE EEEEKSEVIN DEVKVVTGKD GQTGTPVAIA TQLPPKVSAA FSSQQQP FQ QALAGSLVAG AGSTVETDLF KRQQAMPSTG MAEQSKRPRL EVGHQGVVFQ HPGADAGV P LQQLMPTAQG GMPPTPQAAQ LAGQRQSQQQ YDPSTGPPVQ NAASLHTPLP QLPGRLPPA GVPTAALSSA LQFAQQPQVV EAQTQLQIPV KTQQPNVPIP APPSSQLPIP PSQPAQLALH VPTPGKVQV QASQLSSLPQ MVASTRLPVD PAPPCPRPLP TSSTSSLAPV SGSGPGPSPA R SSPVNRPS SATNKALSPV TSRTPGVVAS APTKPQSPAQ NATSSQDSSQ DTLTEQITLE NQ VHQRIAE LRKAGLWSQR RLPKLQEAPR PKSHWDYLLE EMQWMATDFA QERRWKVAAA KKL VRTVVR HHEEKQLREE RGKKEEQSRL RRIAASTARE IECFWSNIEQ VVEIKLRVEL EEKR KKALN LQKVSRRGKE LRPKGFDALQ ESSLDSGMSG RKRKASISLT DDEVDDEEET IEEEE ANEG VVDHQTELSN LAKEAELPLL DLMKLYEGAF LPSSQWPRPK PDGEDTSGEE DADDCP GDR ESRKDLVLID SLFIMDQFKA AERMNIGKPN AKDIADVTAV AEAILPKGSA RVTTSVK FN APSLLYGALR DYQKIGLDWL AKLYRKNLNG ILADEAGLGK TVQIIAFFAH LACNEGNW G PHLVVVRSCN ILKWELELKR WCPGLKILSY IGSHRELKAK RQEWAEPNSF HVCITSYTQ FFRGLTAFTR VRWKCLVIDE MQRVKGMTER HWEAVFTLQS QQRLLLIDSP LHNTFLELWT MVHFLVPGI SRPYLSSPLR APSEESQDYY HKVVIRLHRV TQPFILRRTK RDVEKQLTKK Y EHVLKCRL SNRQKALYED VILQPGTQEA LKSGHFVNVL SILVRLQRIC NHPGLVEPRH PG SSYVAGP LEYPSASLIL KALERDFWKE ADLSMFDLIG LENKITRHEA ELLSKKKIPR KLM EEISTS AAPAARPAAA KLKASRLFQP VQYGQKPEGR TVAFPSTHPP RTAAPTTASA APQG PLRGR PPIATFSANP EAKAAAAPFQ TSQASASAPR HQPASASSTA ASPAHPAKLR AQTTA QAST PGQPPPQPQA PSHAAGQSAL PQRLVLPSQA QARLPSGEVV KIAQLASITG PQSRVA QPE TPVTLQFQGS KFTLSHSQLR QLTAGQPLQL QGSVLQIVSA PGQPYLRAPG PVVMQTV SQ AGAVHGALGS KPPAGGPSPA PLTPQVGVPG RVAVNALAVG EPGTASKPAS PIGGPTQE E KTRLLKERLD QIYLVNERRC SQAPVYGRDL LRICALPSHG RVQWRGSLDG RRGKEAGPA HSYTSSSESP SELMLTLCRC GESLQDVIDR VAFVIPPVVA APPSLRVPRP PPLYSHRMRI LRQGLREHA APYFQQLRQT TAPRLLQFPE LRLVQFDSGK LEALAILLQK LKSEGRRVLI L SQMILMLD ILEMFLNFHY LTYVRIDENA SSEQRQELMR SFNRDRRIFC AILSTHSRTT GI NLVEADT VVFYDNDLNP VMDAKAQEWC DRIGRCKDIH IYRLVSGNSI EEKLLKNGTK DLI REVAAQ GNDYSMAFLT QRTIQELFEV YSPMDDAGFP VKAEEFVVLS QEPSVTETIA PKIA RPFIE ALKSIEYLEE DAQKSAQEGV LGPHTDALSS DSENMPCDEE PSQLEELADF MEQLT PIEK YALNYLELFH TSIEQEKERN SEDAVMTAVR AWEFWNLKTL QEREARLRLE QEEAEL LTY TREDAYSMEY VYEDVDGQTE VMPLWTPPTP PQDDSDIYLD SVMCLMYEAT PIPEAKL PP VYVRKERKRH KTDPSAAGRK KKQRHGEAVV PPRSLFDRAT PGLLKIRREG KEQKKNIL L KQQVPFAKPL PTFAKPTAEP GQDNPEWLIS EDWALLQAVK QLLELPLNLT IVSPAHTPN WDLVSDVVNS CSRIYRSSKQ CRNRYENVII PREEGKSKNN RPLRTSQIYA QDENATHTQL YTSHFDLMK MTAGKRSPPI KPLLGMNPFQ KNPKHASVLA ESGINYDKPL PPIQVASLRA E RIAKEKKA LADQQKAQQP AVAQPPPPQP QPPPPPQQPP PPLPQPQAAG SQPPAGPPAV QP QPQPQPQ TQPQPVQAPA KAQPAITTGG SAAVLAGTIK TSVTGTSMPT GAVSGNVIVN TIA GVPAAT FQSINKRLAS PVAPGALTTP GGSAPAQVVH TQPPPRAVGS PATATPDLVS MATT QGVRA VTSVTASAVV TTNLTPVQTP ARSLVPQVSQ ATGVQLPGKT ITPAHFQLLR QQQQQ QQQQ QQQQQQQQQQ QQQQQQQQQQ TTTTSQVQVP QIQGQAQSPA QIKAVGKLTP EHLIKM QKQ KLQMPPQPPP PQAQSAPPQP TAQVQVQTSQ PPQQQSPQLT TVTAPRPGAL LTGTTVA NL QVARLTRVPT SQLQAQGQMQ TQAPQPAQVA LAKPPVVSVP AAVVSSPGVT TLPMNVAG I SVAIGQPQKA AGQTVVAQPV HMQQLLKLKQ QAVQQQKAIQ PQAAQGPAAV QQKITAQQI TTPGAQQKVA YAAQPALKTQ FLTTPISQAQ KLAGAQQVQT QIQVAKLPQV VQQQTPVASI QQVASASQQ ASPQTVALTQ ATAAGQQVQM IPAVTATAQV VQQKLIQQQV VTTASAPLQT P GAPNPAQV PASSDSPSQQ PKLQMRVPAV RLKTPTKPPC Q

UniProtKB: E1A-binding protein p400

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Macromolecule #2: EPC1

MacromoleculeName: EPC1 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS AQQVYGEKRD NMVIPVPEAE SNIAYYESIY PGEFKMPKQL IHIQPFSLDA EQPDYDLDSE DEVFVNKLKK KMDICPLQFE EMIDRLEKGS GQQPVSLQEA KLLLKEDDEL ...String:
MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS AQQVYGEKRD NMVIPVPEAE SNIAYYESIY PGEFKMPKQL IHIQPFSLDA EQPDYDLDSE DEVFVNKLKK KMDICPLQFE EMIDRLEKGS GQQPVSLQEA KLLLKEDDEL IREVYEYWIK KRKNCRGPSL IPSVKQEKRD GSSTNDPYVA FRRRTEKMQT RKNRKNDEAS YEKMLKLRRD LSRAVTILEM IKRREKSKRE LLHLTLEIME KRYNLGDYNG EIMSEVMAQR QPMKPTYAIP IIPITNSSQF KHQEAMDVKE FKVNKQDKAD LIRPKRKYEK KPKVLPSSAA ATPQQTSPAA LPVFNAKDLN QYDFPSSDEE PLSQVLSGSS EAEEDNDPDG PFAFRRKAGC QYYAPHLDQT GNWPWTSPKD GGLGDVRYRY CLTTLTVPQR CIGFARRRVG RGGRVLLDRA HSDYDSVFHH LDLEMLSSPQ HSPVNQFANT SETNTSDKSF SKDLSQILVN IKSCRWRHFR PRTPSLHDSD NDELSCRKLY RSINRTGTAQ PGTQTCSTST QSKSSSGSAH FAFTAEQYQQ HQQQLALMQK QQLAQIQQQQ ANSNSSTNTS QNLASNQQKS GFRLNIQGLE RTLQGFVSKT LDSASAQFAA SALVTSEQLM GFKMKDDVVL GIGVNGVLPA SGVYKGLHLS STTPTALVHT SPSTAGSALL QPSNITQTSS SHSALSHQVT AANSATTQVL IGNNIRLTVP SSVATVNSIA PINARHIPRT LSAVPSSALK LAAAANCQVS KVPSSSSVDS VPRENHESEK PALNNIADNT VAMEVT

UniProtKB: Enhancer of polycomb homolog 1

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Macromolecule #3: VPS72

MacromoleculeName: VPS72 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK VNTPAGSSQK AREEKALLPL ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE ...String:
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK VNTPAGSSQK AREEKALLPL ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE ELLREAKITE ELNLRSLETY ERLEADKKKQ VHKKRKCPGP IITYHSVTVP LVGEPGPKEE NVDIEGLDPA PSVSALTPHA GTGPVNPPAR CSRTFITFSD DATFEEWFPQ GRPPKVPVRE VCPVTHRPAL YRDPVTDIPY ATARAFKIIR EAYKKYITAH GLPPTASALG PGPPPPEPLP GSGPRALRQK IVIK

UniProtKB: Vacuolar protein sorting-associated protein 72 homolog

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Macromolecule #4: DMAP1

MacromoleculeName: DMAP1 / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP EGMHREVYAL LYSDKKDAPP LLPSDTGQGY RTVKAKLGSK KVRPWKWMPF TNPARKDGAM FFHWRRAAEE GKDYPFARFN KTVQVPVYSE QEYQLYLHDD AWTKAETDHL FDLSRRFDLR ...String:
MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP EGMHREVYAL LYSDKKDAPP LLPSDTGQGY RTVKAKLGSK KVRPWKWMPF TNPARKDGAM FFHWRRAAEE GKDYPFARFN KTVQVPVYSE QEYQLYLHDD AWTKAETDHL FDLSRRFDLR FVVIHDRYDH QQFKKRSVED LKERYYHICA KLANVRAVPG TDLKIPVFDA GHERRRKEQL ERLYNRTPEQ VAEEEYLLQE LRKIEARKKE REKRSQDLQK LITAADTTAE QRRTERKAPK KKLPQKKEAE KPAVPETAGI KFPDFKSAGV TLRSQRMKLP SSVGQKKIKA LEQMLLELGV ELSPTPTEEL VHMFNELRSD LVLLYELKQA CANCEYELQM LRHRHEALAR AGVLGGPATP ASGPGPASAE PAVTEPGLGP DPKDTIIDVV GAPLTPNSRK RRESASSSSS VKKAKKP

UniProtKB: DNA methyltransferase 1-associated protein 1

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Macromolecule #5: ACL6A

MacromoleculeName: ACL6A / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK GKQGGPTYYI DTNALRVPRE NMEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV LMSEAPWNTR AKREKLTELM FEHYNIPAFF LCKTAVLTAF ANGRSTGLIL ...String:
MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK GKQGGPTYYI DTNALRVPRE NMEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV LMSEAPWNTR AKREKLTELM FEHYNIPAFF LCKTAVLTAF ANGRSTGLIL DSGATHTTAI PVHDGYVLQQ GIVKSPLAGD FITMQCRELF QEMNIELVPP YMIASKEAVR EGSPANWKRK EKLPQVTRSW HNYMCNCVIQ DFQASVLQVS DSTYDEQVAA QMPTVHYEFP NGYNCDFGAE RLKIPEGLFD PSNVKGLSGN TMLGVSHVVT TSVGMCDIDI RPGLYGSVIV AGGNTLIQSF TDRLNRELSQ KTPPSMRLKL IANNTTVERR FSSWIGGSIL ASLGTFQQMW ISKQEYEEGG KQCVERKCP

UniProtKB: Actin-like protein 6A

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Macromolecule #6: ACTIN

MacromoleculeName: ACTIN / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA ...String:
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ EYDESGPSIV HRKCF

UniProtKB: Actin, cytoplasmic 1

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Macromolecule #7: RUVBL1

MacromoleculeName: RUVBL1 / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL ...String:
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIFESL QKERVEAGDV IYIEANSGAV KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG IAELVPGVLF VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN GKDSIEKEHV EEISELFYDA KSSAKILADQ QDKYMK

UniProtKB: RuvB-like 1

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Macromolecule #8: RUVBL2

MacromoleculeName: RUVBL2 / type: protein_or_peptide / ID: 8 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET ...String:
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTT PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS

UniProtKB: RuvB-like 2

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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

Concentration0.2 mg/mL
BufferpH: 8
Component:
ConcentrationFormula
20.0 mMHEPES
250.0 mMNaCl
2.0 mMMgCl2
20.0 mMBiotin
1.0 %Trehalose
2.0 mMDTT
0.0125 %DDM
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 90 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 279 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / 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 / Cs: 2.7 mm / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.2 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 284286
Startup modelType of model: OTHER / Details: Ab-initio
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.52 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 180397
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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