+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-18581 | |||||||||
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Title | Human Tip60 complex | |||||||||
Map data | Overall structure | |||||||||
Sample |
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Keywords | Eukaryotic transcription / Histone acetyltransferase / chromatin remodeling / Complex / TRANSCRIPTION | |||||||||
Function / homology | Function and homology information ATP-dependent H2AZ histone chaperone activity / piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / histone chaperone activity / regulation of transepithelial transport / sperm DNA condensation ...ATP-dependent H2AZ histone chaperone activity / piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / histone chaperone activity / regulation of transepithelial transport / sperm DNA condensation / establishment of protein localization to chromatin / morphogenesis of a polarized epithelium / bBAF complex / postsynaptic actin cytoskeleton organization / npBAF complex / nBAF complex / protein localization to adherens junction / postsynaptic actin cytoskeleton / brahma complex / dynein axonemal particle / Tat protein binding / R2TP complex / structural constituent of postsynaptic actin cytoskeleton / RPAP3/R2TP/prefoldin-like complex / chromatin-protein adaptor activity / GBAF complex / regulation of G0 to G1 transition / neural retina development / Formation of annular gap junctions / dense body / Gap junction degradation / Swr1 complex / Cell-extracellular matrix interactions / positive regulation of telomerase RNA localization to Cajal body / Folding of actin by CCT/TriC / apical protein localization / regulation of double-strand break repair / regulation of nucleotide-excision repair / RSC-type complex / adherens junction assembly / Ino80 complex / Prefoldin mediated transfer of substrate to CCT/TriC / blastocyst formation / RHOF GTPase cycle / Adherens junctions interactions / tight junction / enzyme-substrate adaptor activity / Sensory processing of sound by outer hair cells of the cochlea / regulation of mitotic metaphase/anaphase transition / protein folding chaperone complex / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / SWI/SNF complex / positive regulation of double-strand break repair / regulation of norepinephrine uptake / box C/D snoRNP assembly / positive regulation of T cell differentiation / regulation of synaptic vesicle endocytosis / apical junction complex / establishment or maintenance of cell polarity / regulation of cyclin-dependent protein serine/threonine kinase activity / cortical cytoskeleton / maintenance of blood-brain barrier / negative regulation of gene expression, epigenetic / spinal cord development / positive regulation of stem cell population maintenance / regulation of chromosome organization / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of DNA replication / regulation of G1/S transition of mitotic cell cycle / Transcriptional Regulation by E2F6 / somatic stem cell population maintenance / Recycling pathway of L1 / brush border / kinesin binding / calyx of Held / TFIID-class transcription factor complex binding / regulation of embryonic development / negative regulation of cell differentiation / spermatid development / MLL1 complex / Telomere Extension By Telomerase / positive regulation of double-strand break repair via homologous recombination / EPH-ephrin mediated repulsion of cells / positive regulation of myoblast differentiation / RHO GTPases Activate WASPs and WAVEs / regulation of protein localization to plasma membrane / RNA polymerase II core promoter sequence-specific DNA binding / RHO GTPases activate IQGAPs / regulation of DNA repair / histone acetyltransferase activity / Deposition of new CENPA-containing nucleosomes at the centromere / substantia nigra development / EPHB-mediated forward signaling / TBP-class protein binding / positive regulation of DNA repair / telomere maintenance Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.52 Å | |||||||||
Authors | Li 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
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Citation | Journal: Nature / Year: 2024 Title: Structure of 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 impacts chromatin structure via 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 impacts chromatin structure via two enzymatic activities: ATP-dependent exchange of histone H2A/H2B for H2A.Z/H2B and histone acetylation, which in yeast are carried out by two independent complexes, SWR1 and NuA4, respectively. How these activities are merged in humans into one super-complex and what this association entails for their structure, mechanism and recruitment to chromatin is unknown. Here we describe the 2.4-3.3 Å resolution structure of the endogenous human TIP60-C. We find a three lobed architecture composed of SWR1-like (SWR1L) and NuA4-like (NuA4L) parts, that associate with a TRRAP activator-binding module. The huge EP400 subunit harbors the ATPase motor, traverses twice the junction between SWR1L and NuA4L, and constitutes the scaffold of the three-lobed architecture. NuA4L is completely re-arranged compared to its yeast counterpart. TRRAP is flexibly tethered to NuA4L, in stark contrast to its robust connection to the complete opposite side of yeast NuA4. A modeled nucleosome bound to SWR1L, supported by activity tests, suggests that some aspects of the histone exchange mechanism diverge from the yeast example. Furthermore, a fixed actin module, as opposed to the mobile actin subcomplex in SWR1, the flexibility of TRRAP and the weak effect of extra-nucleosomal DNA on exchange activity, lead to a different, activator-based, mode of enlisting TIP60-C to chromatin. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_18581.map.gz | 616.7 MB | EMDB map data format | |
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Header (meta data) | emd-18581-v30.xml emd-18581.xml | 26.9 KB 26.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_18581_fsc.xml | 22.7 KB | Display | FSC data file |
Images | emd_18581.png | 78.8 KB | ||
Masks | emd_18581_msk_1.map | 1.2 GB | Mask map | |
Filedesc metadata | emd-18581.cif.gz | 9.1 KB | ||
Others | emd_18581_half_map_1.map.gz emd_18581_half_map_2.map.gz | 1.1 GB 1.1 GB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18581 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18581 | HTTPS FTP |
-Validation report
Summary document | emd_18581_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_18581_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_18581_validation.xml.gz | 30.5 KB | Display | |
Data in CIF | emd_18581_validation.cif.gz | 39.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18581 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18581 | HTTPS FTP |
-Related structure data
Related structure data | 8qr1C 8qriC 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_18581.map.gz / Format: CCP4 / Size: 1.2 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Overall structure | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.73 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_18581_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: Half map A
File | emd_18581_half_map_1.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map B
File | emd_18581_half_map_2.map | ||||||||||||
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Annotation | Half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Tip60 complex
Entire | Name: Tip60 complex |
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Components |
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-Supramolecule #1: Tip60 complex
Supramolecule | Name: Tip60 complex / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) / Strain: K562 |
-Macromolecule #1: EP400
Macromolecule | Name: EP400 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Sequence | String: 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: UNIPROTKB: Q96L91 |
-Macromolecule #2: EPC1
Macromolecule | Name: EPC1 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #3: VPS72
Macromolecule | Name: VPS72 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #4: DMAP1
Macromolecule | Name: DMAP1 / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #5: ACL6A
Macromolecule | Name: ACL6A / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #6: ACTIN
Macromolecule | Name: ACTIN / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #7: RUVBL1
Macromolecule | Name: RUVBL1 / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #8: RUVBL2
Macromolecule | Name: RUVBL2 / type: protein_or_peptide / ID: 8 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.2 mg/mL | ||||||||||||||||
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Buffer | pH: 8 Component:
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Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 90 sec. | ||||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 279 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.2 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |