[English] 日本語
Yorodumi
- EMDB-32149: TRA module of NuA4 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-32149
TitleTRA module of NuA4
Map dataTRA1 module
Sample
  • Complex: TRA1 module of NuA4
    • Protein or peptide: Chromatin modification-related protein EAF1
    • Protein or peptide: Actin-related protein 4
    • Protein or peptide: Actin
    • Protein or peptide: SWR1-complex protein 4
    • Protein or peptide: Enhancer of polycomb-like protein 1
    • Protein or peptide: Transcription-associated protein 1
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
KeywordsNuA4 Tra1 / DNA BINDING PROTEIN
Function / homology
Function and homology information


RHOB GTPase cycle / RHOA GTPase cycle / cellular bud neck contractile ring / piccolo histone acetyltransferase complex / ascospore wall assembly / vacuole inheritance / actin cortical patch / mitotic actomyosin contractile ring contraction / Swr1 complex / SLIK (SAGA-like) complex ...RHOB GTPase cycle / RHOA GTPase cycle / cellular bud neck contractile ring / piccolo histone acetyltransferase complex / ascospore wall assembly / vacuole inheritance / actin cortical patch / mitotic actomyosin contractile ring contraction / Swr1 complex / SLIK (SAGA-like) complex / kinetochore assembly / Ino80 complex / SAGA complex / SWI/SNF complex / establishment of cell polarity / NuA4 histone acetyltransferase complex / actin filament bundle / positive regulation of macroautophagy / protein secretion / chromosome organization / Ub-specific processing proteases / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / endocytosis / transcription corepressor activity / nucleosome / chromatin organization / histone binding / protein-containing complex assembly / hydrolase activity / chromatin remodeling / cell cycle / DNA repair / DNA-templated transcription / chromatin binding / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / ATP binding / identical protein binding / nucleus
Similarity search - Function
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 / Tra1, HEAT repeat ring region / Tra1, HEAT repeat central region / Tra1 HEAT repeat central region / Tra1 HEAT repeat ring region / Myb-like domain profile. / domain in helicases and associated with SANT domains ...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 / Tra1, HEAT repeat ring region / Tra1, HEAT repeat central region / Tra1 HEAT repeat central region / Tra1 HEAT repeat ring region / Myb-like domain profile. / domain in helicases and associated with SANT domains / Myb-like DNA-binding domain / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / PIK-related kinase, FAT / FAT domain / FATC domain / PIK-related kinase / FAT domain profile. / FATC domain profile. / Enhancer of polycomb-like, N-terminal / Enhancer of polycomb-like / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic 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 / Homeobox-like domain superfamily / ATPase, nucleotide binding domain / Armadillo-type fold / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Transcription-associated protein 1 / Enhancer of polycomb-like protein 1 / SWR1-complex protein 4 / Actin / Actin-related protein 4 / Chromatin modification-related protein EAF1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Saccharomyces cerevisiae S288C (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsChen Z / Qu K
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nature / Year: 2022
Title: Structure of the NuA4 acetyltransferase complex bound to the nucleosome.
Authors: Keke Qu / Kangjing Chen / Hao Wang / Xueming Li / Zhucheng Chen /
Abstract: Deoxyribonucleic acid in eukaryotes wraps around the histone octamer to form nucleosomes, the fundamental unit of chromatin. The N termini of histone H4 interact with nearby nucleosomes and play an ...Deoxyribonucleic acid in eukaryotes wraps around the histone octamer to form nucleosomes, the fundamental unit of chromatin. The N termini of histone H4 interact with nearby nucleosomes and play an important role in the formation of high-order chromatin structure and heterochromatin silencing. NuA4 in yeast and its homologue Tip60 complex in mammalian cells are the key enzymes that catalyse H4 acetylation, which in turn regulates chromatin packaging and function in transcription activation and DNA repair. Here we report the cryo-electron microscopy structure of NuA4 from Saccharomyces cerevisiae bound to the nucleosome. NuA4 comprises two major modules: the catalytic histone acetyltransferase (HAT) module and the transcription activator-binding (TRA) module. The nucleosome is mainly bound by the HAT module and is positioned close to a polybasic surface of the TRA module, which is important for the optimal activity of NuA4. The nucleosomal linker DNA carrying the upstream activation sequence is oriented towards the conserved, transcription activator-binding surface of the Tra1 subunit, which suggests a potential mechanism of NuA4 to act as a transcription co-activator. The HAT module recognizes the disk face of the nucleosome through the H2A-H2B acidic patch and nucleosomal DNA, projecting the catalytic pocket of Esa1 to the N-terminal tail of H4 and supporting its function in selective acetylation of H4. Together, our findings illustrate how NuA4 is assembled and provide mechanistic insights into nucleosome recognition and transcription co-activation by a HAT.
History
DepositionNov 9, 2021-
Header (metadata) releaseAug 10, 2022-
Map releaseAug 10, 2022-
UpdateJun 26, 2024-
Current statusJun 26, 2024Processing site: PDBj / Status: Released

-
Structure visualization

Supplemental images

emd_32149.png

Downloads & links

-
Map

FileDownload / File: emd_32149.map.gz / Format: CCP4 / Size: 202.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationTRA1 module
Voxel sizeX=Y=Z: 1.0825 Å
Density
Contour LevelBy AUTHOR: 0.013
Minimum - Maximum-0.027050894 - 0.063032016
Average (Standard dev.)0.00015041292 (±0.0014817263)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions376376376
Spacing376376376
CellA=B=C: 407.02 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

-
Entire : TRA1 module of NuA4

EntireName: TRA1 module of NuA4
Components
  • Complex: TRA1 module of NuA4
    • Protein or peptide: Chromatin modification-related protein EAF1
    • Protein or peptide: Actin-related protein 4
    • Protein or peptide: Actin
    • Protein or peptide: SWR1-complex protein 4
    • Protein or peptide: Enhancer of polycomb-like protein 1
    • Protein or peptide: Transcription-associated protein 1
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

-
Supramolecule #1: TRA1 module of NuA4

SupramoleculeName: TRA1 module of NuA4 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

-
Macromolecule #1: Chromatin modification-related protein EAF1

MacromoleculeName: Chromatin modification-related protein EAF1 / 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: 133.949953 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSSRPSSAVP NSASLSEDQS SDRSKFPKAD DLIDERDRKL TELYCVSRLN QLLELTDENK LRKEIDAFLK KNDIRRGIRF DEASLPKLL HTAATPITKK KLKDVNLINV PNQRLSDSKM SRELPENSEN VSVKSESHFV PSHDNSIREN MMDSLRPAEK T GGMWNKRP ...String:
MSSRPSSAVP NSASLSEDQS SDRSKFPKAD DLIDERDRKL TELYCVSRLN QLLELTDENK LRKEIDAFLK KNDIRRGIRF DEASLPKLL HTAATPITKK KLKDVNLINV PNQRLSDSKM SRELPENSEN VSVKSESHFV PSHDNSIREN MMDSLRPAEK T GGMWNKRP LESTMGGEEE RHEKRQKMQS QSLESSNNSE MASLPISPRP PVPNALAHYT YYENIEYPPA DPTEVQPAVK FK DPLIKNI MAKEIDTSDH YNENNVDALE TVFLLMNDYI PSKIPQALPL AELKYMSQTL PLINLIPRAH KALTTNIINN ALN EARITV VGSRIEELRR LGLWSLRQPK RFIDPWKQHN THQNILLEEA KWMQADFKEG HKYKVAICTA MAQAIKDYWT YGEI CCVKR KTLLPGKENK LSDDGRISEK SGRPSDTSRN DSDISIAGKD DIGIIANVDD ITEKESAAAN DNDENGKNEA GAKSD FDFA DGLLSQEGAH DQIISSIDTK LLLKKPSSSS EVVLIQHEVA ASSALIETEE SKKELAPPFK LSIFVDELNT FEKTLI QDL PLYNGINEER PKKDDSLPFI PISKSVVSLD DNGFYKLLER QLIDEEPSIS QLSKRRGMFY GNRRNHYLRP PAVPSLR YL QNRTPTIWLS EDDQELVKNI NTYGYNWELI SAHMTHRLTY SYLSNIERRT PWQCFERFVQ LNERFNFSDL KGPRAHSA Q QWLIEAHKFQ QRQNRRISPL GVNTESIQRG HRRLRWASMF EAIRKCMKKR ENTPRPNPTQ PRKPLDCKNM KVPTPAEMS LLKAQRDEAL RRDIQLRRTV KNRLQQRQQQ SQQAHSSRAQ SPIPSNGKSS SNLARNGQAS APRPNQKQYT EQDIIESYSR KLLEQKPDI GPEMALKAAK NYYRTLREQQ QQLKQHQIQQ QRQQLQEESS HVQQLQQLQP GSQAPPPKSS PSQSSLSNIS N INSAPRIK SPTPQEILQR FQKQRTLQVD WSHPQFEKHH HHHHHHHHHH DYDIPTTASV DGSENLYFQG SPQQNKTAAL AQ HDEAVDN KFNKEQQNAF YEILHLPNLN EEQRNAFIQS LKDDPSQSAN LLAEAKKLND AQAPKVDNKF NKEQQNAFYE ILH LPNLNE EQRNAFIQSL KDDPSQSANL LAEAKKLNDA QAPKVDANSA AL

UniProtKB: Chromatin modification-related protein EAF1

-
Macromolecule #2: Actin-related protein 4

MacromoleculeName: Actin-related protein 4 / 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: 54.894684 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSNAALQVYG GDEVSAVVID PGSYTTNIGY SGSDFPQSIL PSVYGKYTAD EGNKKIFSEQ SIGIPRKDYE LKPIIENGLV IDWDTAQEQ WQWALQNELY LNSNSGIPAL LTEPVWNSTE NRKKSLEVLL EGMQFEACYL APTSTCVSFA AGRPNCLVVD I GHDTCSVS ...String:
MSNAALQVYG GDEVSAVVID PGSYTTNIGY SGSDFPQSIL PSVYGKYTAD EGNKKIFSEQ SIGIPRKDYE LKPIIENGLV IDWDTAQEQ WQWALQNELY LNSNSGIPAL LTEPVWNSTE NRKKSLEVLL EGMQFEACYL APTSTCVSFA AGRPNCLVVD I GHDTCSVS PIVDGMTLSK STRRNFIAGK FINHLIKKAL EPKEIIPLFA IKQRKPEFIK KTFDYEVDKS LYDYANNRGF FQ ECKETLC HICPTKTLEE TKTELSSTAK RSIESPWNEE IVFDNETRYG FAEELFLPKE DDIPANWPRS NSGVVKTWRN DYV PLKRTK PSGVNKSDKK VTPTEEKEQE AVSKSTSPAA NSADTPNETG KRPLEEEKPP KENNELIGLA DLVYSSIMSS DVDL RATLA HNVVLTGGTS SIPGLSDRLM TELNKILPSL KFRILTTGHT IERQYQSWLG GSILTSLGTF HQLWVGKKEY EEVGV ERLL NDRFR

UniProtKB: Actin-related protein 4

-
Macromolecule #3: Actin

MacromoleculeName: Actin / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 41.735547 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS KRGILTLRYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP MNPKSNREKM TQIMFETFNV PAFYVSIQAV LSLYSSGRTT GIVLDSGDGV T HVVPIYAG ...String:
MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS KRGILTLRYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP MNPKSNREKM TQIMFETFNV PAFYVSIQAV LSLYSSGRTT GIVLDSGDGV T HVVPIYAG FSLPHAILRI DLAGRDLTDY LMKILSERGY SFSTTAEREI VRDIKEKLCY VALDFEQEMQ TAAQSSSIEK SY ELPDGQV ITIGNERFRA PEALFHPSVL GLESAGIDQT TYNSIMKCDV DVRKELYGNI VMSGGTTMFP GIAERMQKEI TAL APSSMK VKIIAPPERK YSVWIGGSIL ASLTTFQQMW ISKQEYDESG PSIVHHKCF

UniProtKB: Actin

-
Macromolecule #4: SWR1-complex protein 4

MacromoleculeName: SWR1-complex protein 4 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 55.297684 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSSSDIFDVL NIKQKSRSPT NGQVSVPSSS AANRPKPQVT GMQRELFNLL GENQPPVVIK SGNNFKEKML STSKPSPWSF VEFKANNSV TLRHWVKGSK ELIGDTPKES PYSKFNQHLS IPSFTKEEYE AFMNENEGTQ KSVESEKNHN ENFTNEKKDE S KNSWSFEE ...String:
MSSSDIFDVL NIKQKSRSPT NGQVSVPSSS AANRPKPQVT GMQRELFNLL GENQPPVVIK SGNNFKEKML STSKPSPWSF VEFKANNSV TLRHWVKGSK ELIGDTPKES PYSKFNQHLS IPSFTKEEYE AFMNENEGTQ KSVESEKNHN ENFTNEKKDE S KNSWSFEE IEYLFNLCKK YDLRWFLIFD RYSYNNSRTL EDLKEKFYYT CRNYFKASDP SNPLLSSLNF SAEKEIERKK YL QRLLSRS AAEIAEEEAL VVESKKFEMA AKRTLAERES LLRLLDSPHS DQTITQYLTS QGMSQLYNAL LADKTRKRKH DLN IPENPW MKQQQQFAQH RQLQQLNVKK SEVKENLSPK KTKRQRQEMQ TALKRKSESA YAEQLLKDFN SDERKALGVI THGE KLSPG VYLRSTKLST FKPALQNKIL AILQELSLPS RPVMPSFDVM ERQEELLKKI NTLIDLKKHV DKYEAGMSIT K

UniProtKB: SWR1-complex protein 4

-
Macromolecule #5: Enhancer of polycomb-like protein 1

MacromoleculeName: Enhancer of polycomb-like protein 1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Molecular weightTheoretical: 96.889867 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MPTPSNAIEI NDGSHKSGRS TRRSGSRSAH DDGLDSFSKG DSGAGASAGS SNSRFRHRKI SVKQHLKIYL PNDLKHLDKD ELQQREVVE IETGVEKNEE KEVHLHRILQ MGSGHTKHKD YIPTPDASMT WNEYDKFYTG SFQETTSYIK FSATVEDCCG T NYNMDERD ...String:
MPTPSNAIEI NDGSHKSGRS TRRSGSRSAH DDGLDSFSKG DSGAGASAGS SNSRFRHRKI SVKQHLKIYL PNDLKHLDKD ELQQREVVE IETGVEKNEE KEVHLHRILQ MGSGHTKHKD YIPTPDASMT WNEYDKFYTG SFQETTSYIK FSATVEDCCG T NYNMDERD ETFLNEQVNK GSSDILTEDE FEILCSSFEH AIHERQPFLS MDPESILSFE ELKPTLIKSD MADFNLRNQL NH EINSHKT HFITQFDPVS QMNTRPLIQL IEKFGSKIYD YWRERKIEVN GYEIFPQLKF ERPGEKEEID PYVCFRRREV RHP RKTRRI DILNSQRLRA LHQELKNAKD LALLVAKREN VSLNWINDEL KIFDQRVKIK NLKRSLNISG EDDDLINHKR KRPT IVTVE QREAELRKAE LKRAAAAAAA AKAKNNKRNN QLEDKSSRLT KQQQQQLLQQ QQQQQQNALK TENGKQLANA SSSST SQPI TSHVYVKLPS SKIPDIVLED VDALLNSKEK NARKFVQEKM EKRKIEDADV FFNLTDDPFN PVFDMSLPKN FSTSNV PFA SIASSKFQID RSFYSSHLPE YLKGISDDIR IYDSNGRSRN KDNYNLDTKR IKKTELYDPF QENLEIHSRE YPIKFRK RV GRSNIKYVDR MPNFTTSSTK SACSLMDFVD FDSIEKEQYS REGSNDTDSI NVYDSKYDEF VRLYDKWKYD SPQNEYGI K FSDEPARLNQ ISNDTQVIRF GTMLGTKSYE QLREATIKYR RDYITRLKQK HIQHLQQQQQ QQQQQQQQAQ QQKQKSQNN NSNSSNSLKK LNDSLINSEA KQNSSITQKN SS

UniProtKB: Enhancer of polycomb-like protein 1

-
Macromolecule #6: Transcription-associated protein 1

MacromoleculeName: Transcription-associated protein 1 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 433.677281 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSLTEQIEQF ASRFRDDDAT LQSRYSTLSE LYDIMELLNS PEDYHFFLQA VIPLLLNQLK EVPISYDAHS PEQKLRNSML DIFNRCLMN QTFQPYAMEV LEFLLSVLPK ENEENGILCM KVLTTLFKSF KSILQDKLDS FIRIIIQIYK NTPNLINQTF Y EAGKAEQG ...String:
MSLTEQIEQF ASRFRDDDAT LQSRYSTLSE LYDIMELLNS PEDYHFFLQA VIPLLLNQLK EVPISYDAHS PEQKLRNSML DIFNRCLMN QTFQPYAMEV LEFLLSVLPK ENEENGILCM KVLTTLFKSF KSILQDKLDS FIRIIIQIYK NTPNLINQTF Y EAGKAEQG DLDSPKEPQA DELLDEFSKN DEEKDFPSKQ SSTEPRFENS TSSNGLRSSM FSFKILSECP ITMVTLYSSY KQ LTSTSLP EFTPLIMNLL NIQIKQQQEA REQAESRGEH FTSISTEIIN RPAYCDFILA QIKATSFLAY VFIRGYAPEF LQD YVNFVP DLIIRLLQDC PSELSSARKE LLHATRHILS TNYKKLFLPK LDYLFDERIL IGNGFTMHET LRPLAYSTVA DFIH NIRSE LQLSEIEKTI KIYTGYLLDE SLALTVQIMS AKLLLNLVER ILKLGKENPQ EAPRAKKLLM IIIDSYMNRF KTLNR QYDT IMKYYGRYET HKKEKAEKLK NSIQDNDKES EEFMRKVLEP SDDDHLMPQP KKEDINDSPD VEMTESDKVV KNDVEM FDI KNYAPILLLP TPTNDPIKDA FYLYRTLMSF LKTIIHDLKV FNPPPNEYTV ANPKLWASVS RVFSYEEVIV FKDLFHE CI IGLKFFKDHN EKLSPETTKK HFDISMPSLP VSATKDAREL MDYLAFMFMQ MDNATFNEII EQELPFVYER MLEDSGLL H VAQSFLTSEI TSPNFAGILL RFLKGKLKDL GNVDFNTSNV LIRLFKLSFM SVNLFPNINE VVLLPHLNDL ILNSLKYST TAEEPLVYFY LIRTLFRSIG GGRFENLYRS IKPILQVLLQ SLNQMILTAR LPHERELYVE LCITVPVRLS VLAPYLPFLM KPLVFALQQ YPDLVSQGLR TLELCIDNLT AEYFDPIIEP VIDDVSKALF NLLQPQPFNH AISHNVVRIL GKLGGRNRQF L KPPTDLTE KTELDIDAIA DFKINGMPED VPLSVTPGIQ SALNILQSYK SDIHYRKSAY KYLTCVLLLM TKSSAEFPTN YT ELLKTAV NSIKLERIGI EKNFDLEPTV NKRDYSNQEN LFLRLLESVF YATSIKELKD DAMDLLNNLL DHFCLLQVNT TLL NKRNYN GTFNIDLKNP NFMLDSSLIL DAIPFALSYY IPEVREVGVL AYKRIYEKSC LIYGEELALS HSFIPELAKQ FIHL CYDET YYNKRGGVLG IKVLIDNVKS SSVFLKKYQY NLANGLLFVL KDTQSEAPSA ITDSAEKLLI DLLSITFADV KEEDL GNKV LENTLTDIVC ELSNANPKVR NACQKSLHTI SNLTGIPIVK LMDHSKQFLL SPIFAKPLRA LPFTMQIGNV DAITFC LSL PNTFLTFNEE LFRLLQESIV LADAEDESLS TNIQKTTEYS TSEQLVQLRI ACIKLLAIAL KNEEFATAQQ GNIRIRI LA VFFKTMLKTS PEIINTTYEA LKGSLAENSK LPKELLQNGL KPLLMNLSDH QKLTVPGLDA LSKLLELLIA YFKVEIGR K LLDHLTAWCR VEVLDTLFGQ DLAEQMPTKI IVSIINIFHL LPPQADMFLN DLLLKVMLLE RKLRLQLDSP FRTPLARYL NRFHNPVTEY FKKNMTLRQL VLFMCNIVQR PEAKELAEDF EKELDNFYDF YISNIPKNQV RVVSFFTNMV DLFNTMVITN GDEWLKKKG NMILKLKDML NLTLKTIKEN SFYIDHLQLN QSIAKFQALY LRFTELSERD QNPLLLDFID FSFSNGIKAS Y SLKKFIFH NIIASSNKEK QNNFINDATL FVLSDKCLDA RIFVLKNVIN STLIYEVATS GSLKSYLVED KKPKWLELLH NK IWKNSNA ILAYDVLDHH DLFRFELLQL SAIFIKADPE IIAEIKKDII KFCWNFIKLE DTLIKQSAYL VTSYFISKFD FPI KVVTQV FVALLRSSHV EARYLVKQSL DVLTPVLHER MNAAGTPDTW INWVKRVMVE NSSSQNNILY QFLISHPDLF FNSR DLFIS NIIHHMNKIT FMSNSNSDSH TLAIDLASLI LYWENKTLEI TNVNNTKTDS DGDVVMSDSK SDINPVEADT TAIIV DANN NSPISLHLRE ACTAFLIRYV CASNHRAIET ELGLRAINIL SELISDKHWT NVNVKLVYFE KFLIFQDLDS ENILYY CMN ALDVLYVFFK NKTKEWIMEN LPTIQNLLEK CIKSDHHDVQ EALQKVLQVI MKAIKAQGVS VIIEEESPGK TFIQMLT SV ITQDLQETSS VTAGVTLAWV LFMNFPDNIV PLLTPLMKTF SKLCKDHLSI SQPKDAMALE EARITTKLLE KVLYILSL K VSLLGDSRRP FLSTVALLID HSMDQNFLRK IVNMSRSWIF NTEIFPTVKE KAAILTKMLA FEIRGEPSLS KLFYEIVLK LFDQEHFNNT EITVRMEQPF LVGTRVEDIG IRKRFMTILD NSLERDIKER LYYVIRDQNW EFIADYPWLN QALQLLYGSF NREKELSLK NIYCLSPPSI LQEYLPENAE MVTEVNDLEL SNFVKGHIAS MQGLCRIISS DFIDSLIEIF YQDPKAIHRA W VTLFPQVY KSIPKNEKYG FVRSIITLLS KPYHTRQISS RTNVINMLLD SISKIESLEL PPHLVKYLAI SYNAWYQSIN IL ESIQSNT SIDNTKIIEA NEDALLELYV NLQEEDMFYG LWRRRAKYTE TNIGLSYEQI GLWDKAQQLY EVAQVKARSG ALP YSQSEY ALWEDNWIQC AEKLQHWDVL TELAKHEGFT DLLLECGWRV ADWNSDRDAL EQSVKSVMDV PTPRRQMFKT FLAL QNFAE SRKGDQEVRK LCDEGIQLSL IKWVSLPIRY TPAHKWLLHG FQQYMEFLEA TQIYANLHTT TVQNLDSKAQ EIKRI LQAW RDRLPNTWDD VNMWNDLVTW RQHAFQVINN AYLPLIPALQ QSNSNSNINT HAYRGYHEIA WVINRFAHVA RKHNMP DVC ISQLARIYTL PNIEIQEAFL KLREQAKCHY QNMNELTTGL DVISNTNLVY FGTVQKAEFF TLKGMFLSKL RAYEEAN QA FATAVQIDLN LAKAWAQWGF FNDRRLSEEP NNISFASNAI SCYLQAAGLY KNSKIRELLC RILWLISIDD ASGMLTNA F DSFRGEIPVW YWITFIPQLL TSLSHKEANM VRHILIRIAK SYPQALHFQL RTTKEDFAVI QRQTMAVMGD KPDTNDRNG RRQPWEYLQE LNNILKTAYP LLALSLESLV AQINDRFKST TDEDLFRLIN VLLIDGTLNY NRLPFPRKNP KLPENTEKNL VKFSTTLLA PYIRPKFNAD FIDNKPDYET YIKRLRYWRR RLENKLDRAS KKENLEVLCP HLSNFHHQKF EDIEIPGQYL L NKDNNVHF IKIARFLPTV DFVRGTHSSY RRLMIRGHDG SVHSFAVQYP AVRHSRREER MFQLYRLFNK SLSKNVETRR RS IQFNLPI AIPLSPQVRI MNDSVSFTTL HEIHNEFCKK KGFDPDDIQD FMADKLNAAH DDALPAPDMT ILKVEIFNSI QTM FVPSNV LKDHFTSLFT QFEDFWLFRK QFASQYSSFV FMSYMMMINN RTPHKIHVDK TSGNVFTLEM LPSRFPYERV KPLL KNHDL SLPPDSPIFH NNEPVPFRLT PNIQSLIGDS ALEGIFAVNL FTISRALIEP DNELNTYLAL FIRDEIISWF SNLHR PIIE NPQLREMVQT NVDLIIRKVA QLGHLNSTPT VTTQFILDCI GSAVSPRNLA RTDVNFMPWF

UniProtKB: Transcription-associated protein 1

-
Macromolecule #7: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 7 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

-
Macromolecule #8: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 8 / Number of copies: 2 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.6
VitrificationCryogen name: NITROGEN

-
Electron microscopy

MicroscopeFEI TITAN
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm

+
Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 69770
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more