[English] 日本語
Yorodumi
- EMDB-22587: Structure of TFIIH in TFIIH/Rad4-Rad23-Rad33 DNA opening complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-22587
TitleStructure of TFIIH in TFIIH/Rad4-Rad23-Rad33 DNA opening complex
Map dataStructure of TFIIH in TFIIH/Rad4-Rad23-Rad33 DNA opening complex
Sample
  • Complex: Ternary complex of TFIIH/Rad4-Rad23-Rad33 with AAF damaged DNA
    • Protein or peptide: General transcription and DNA repair factor IIH subunit TFB1
    • Protein or peptide: General transcription and DNA repair factor IIH subunit TFB4
    • Protein or peptide: DNA repair helicase RAD25
    • Protein or peptide: RNA polymerase II transcription factor B subunit 5
    • Protein or peptide: General transcription and DNA repair factor IIH subunit TFB2
    • Protein or peptide: DNA repair helicase RAD3
    • Protein or peptide: General transcription and DNA repair factor IIH subunit SSL1
  • Ligand: ZINC ION
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
Function / homology
Function and homology information


regulation of mitotic recombination / RNA polymerase II promoter clearance / phosphatidylinositol-5-phosphate binding / positive regulation of mitotic recombination / DNA translocase activity / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / transcription open complex formation at RNA polymerase II promoter / phosphatidylinositol-3-phosphate binding / 5'-3' DNA helicase activity ...regulation of mitotic recombination / RNA polymerase II promoter clearance / phosphatidylinositol-5-phosphate binding / positive regulation of mitotic recombination / DNA translocase activity / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / transcription open complex formation at RNA polymerase II promoter / phosphatidylinositol-3-phosphate binding / 5'-3' DNA helicase activity / transcription factor TFIIH holo complex / transcription factor TFIIH core complex / 3'-5' DNA helicase activity / transcription preinitiation complex / poly(A)+ mRNA export from nucleus / DNA duplex unwinding / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / Formation of TC-NER Pre-Incision Complex / RNA Polymerase I Promoter Escape / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Polymerase II Pre-transcription Events / Dual incision in TC-NER / ATPase activator activity / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription by RNA polymerase I / ATP-dependent activity, acting on DNA / DNA helicase activity / transcription initiation at RNA polymerase II promoter / nucleotide-excision repair / ubiquitin protein ligase activity / 4 iron, 4 sulfur cluster binding / double-stranded DNA binding / DNA helicase / transcription by RNA polymerase II / damaged DNA binding / DNA repair / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / zinc ion binding / ATP binding / metal ion binding / nucleus / cytosol
Similarity search - Function
Bacterial type XPD DNA helicase, FeS cluster domain / TFIIH subunit Tfb4/GTF2H3 / Transcription factor Tfb4 / TFIIH C1-like domain / Ssl1-like / TFIIH subunit Ssl1/p44 / Ssl1-like / TFIIH C1-like domain / TFIIH C1-like domain / TFIIH p62 subunit, N-terminal ...Bacterial type XPD DNA helicase, FeS cluster domain / TFIIH subunit Tfb4/GTF2H3 / Transcription factor Tfb4 / TFIIH C1-like domain / Ssl1-like / TFIIH subunit Ssl1/p44 / Ssl1-like / TFIIH C1-like domain / TFIIH C1-like domain / TFIIH p62 subunit, N-terminal / TFIIH subunit Tfb1/GTF2H1 / TFIIH p62 subunit, N-terminal domain / BSD domain / BSD domain superfamily / BSD domain / BSD domain profile. / domain in transcription factors and synapse-associated proteins / RAD3/XPD family / Helicase XPB/Ssl2 / Helical and beta-bridge domain / ERCC3/RAD25/XPB helicase, C-terminal domain / Helicase XPB/Ssl2, N-terminal domain / Helical and beta-bridge domain / Helicase conserved C-terminal domain / ERCC3/RAD25/XPB C-terminal helicase / Transcription factor TFIIH subunit p52/Tfb2 / ATP-dependent helicase Rad3/Chl1-like / Transcription factor Tfb2, C-terminal domain / Transcription factor Tfb2 / Transcription factor Tfb2 (p52) C-terminal domain / TFIIH subunit TTDA/Tfb5 / TFB5-like superfamily / Transcription factor TFIIH complex subunit Tfb5 / Transcription factor TFIIH complex subunit Tfb5 / Helicase superfamily 1/2, DinG/Rad3-like / Helicase-like, DEXD box c2 type / ATP-dependent helicase, C-terminal / DEAD2 / Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type / DEAD_2 / Helicase C-terminal domain / Superfamilies 1 and 2 helicase ATP-binding type-2 domain profile. / DEXDc2 / HELICc2 / Helicase/UvrB, N-terminal / Type III restriction enzyme, res subunit / DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site / DEAH-box subfamily ATP-dependent helicases signature. / C1-like domain superfamily / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily / Zinc finger C2H2-type / 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 / PH-like domain superfamily / Zinc finger, RING/FYVE/PHD-type / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
General transcription and DNA repair factor IIH helicase subunit XPD / General transcription and DNA repair factor IIH subunit TFB1 / General transcription and DNA repair factor IIH helicase subunit XPB / General transcription and DNA repair factor IIH subunit TFB2 / General transcription and DNA repair factor IIH subunit SSL1 / General transcription and DNA repair factor IIH subunit TFB4 / General transcription and DNA repair factor IIH subunit TFB5
Similarity search - Component
Biological speciesBaker's yeast (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
Authorsvan Eeuwen T / Min JH / Murakami K
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-GM123233 United States
CitationJournal: Nat Commun / Year: 2021
Title: Cryo-EM structure of TFIIH/Rad4-Rad23-Rad33 in damaged DNA opening in nucleotide excision repair.
Authors: Trevor van Eeuwen / Yoonjung Shim / Hee Jong Kim / Tingting Zhao / Shrabani Basu / Benjamin A Garcia / Craig D Kaplan / Jung-Hyun Min / Kenji Murakami /
Abstract: The versatile nucleotide excision repair (NER) pathway initiates as the XPC-RAD23B-CETN2 complex first recognizes DNA lesions from the genomic DNA and recruits the general transcription factor ...The versatile nucleotide excision repair (NER) pathway initiates as the XPC-RAD23B-CETN2 complex first recognizes DNA lesions from the genomic DNA and recruits the general transcription factor complex, TFIIH, for subsequent lesion verification. Here, we present a cryo-EM structure of an NER initiation complex containing Rad4-Rad23-Rad33 (yeast homologue of XPC-RAD23B-CETN2) and 7-subunit coreTFIIH assembled on a carcinogen-DNA adduct lesion at 3.9-9.2 Å resolution. A ~30-bp DNA duplex could be mapped as it straddles between Rad4 and the Ssl2 (XPB) subunit of TFIIH on the 3' and 5' side of the lesion, respectively. The simultaneous binding with Rad4 and TFIIH was permitted by an unwinding of DNA at the lesion. Translocation coupled with torque generation by Ssl2 and Rad4 would extend the DNA unwinding at the lesion and deliver the damaged strand to Rad3 (XPD) in an open form suitable for subsequent lesion scanning and verification.
History
DepositionSep 2, 2020-
Header (metadata) releaseJul 28, 2021-
Map releaseJul 28, 2021-
UpdateJul 28, 2021-
Current statusJul 28, 2021Processing site: RCSB / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.00593
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.00593
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-7k01
  • Surface level: 0.00593
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22587.png

Downloads & links

-
Map

FileDownload / File: emd_22587.map.gz / Format: CCP4 / Size: 226.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationStructure of TFIIH in TFIIH/Rad4-Rad23-Rad33 DNA opening complex
Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.00593 / Movie #1: 0.00593
Minimum - Maximum-0.016100932 - 0.06109759
Average (Standard dev.)-2.3827126e-05 (±0.0011857244)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions390390390
Spacing390390390
CellA=B=C: 323.69998 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.830.830.83
M x/y/z390390390
origin x/y/z0.0000.0000.000
length x/y/z323.700323.700323.700
α/β/γ90.00090.00090.000
start NX/NY/NZ1331310
NX/NY/NZ223226424
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS390390390
D min/max/mean-0.0160.061-0.000

-
Supplemental data

-
Additional map: Additional map

Fileemd_22587_additional_1.map
AnnotationAdditional map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: half-volume 1

Fileemd_22587_half_map_1.map
Annotationhalf-volume 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: half-volume 2

Fileemd_22587_half_map_2.map
Annotationhalf-volume 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

+
Entire : Ternary complex of TFIIH/Rad4-Rad23-Rad33 with AAF damaged DNA

EntireName: Ternary complex of TFIIH/Rad4-Rad23-Rad33 with AAF damaged DNA
Components
  • Complex: Ternary complex of TFIIH/Rad4-Rad23-Rad33 with AAF damaged DNA
    • Protein or peptide: General transcription and DNA repair factor IIH subunit TFB1
    • Protein or peptide: General transcription and DNA repair factor IIH subunit TFB4
    • Protein or peptide: DNA repair helicase RAD25
    • Protein or peptide: RNA polymerase II transcription factor B subunit 5
    • Protein or peptide: General transcription and DNA repair factor IIH subunit TFB2
    • Protein or peptide: DNA repair helicase RAD3
    • Protein or peptide: General transcription and DNA repair factor IIH subunit SSL1
  • Ligand: ZINC ION
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster

+
Supramolecule #1: Ternary complex of TFIIH/Rad4-Rad23-Rad33 with AAF damaged DNA

SupramoleculeName: Ternary complex of TFIIH/Rad4-Rad23-Rad33 with AAF damaged DNA
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7
Molecular weightExperimental: 420 kDa/nm

+
Macromolecule #1: General transcription and DNA repair factor IIH subunit TFB1

MacromoleculeName: General transcription and DNA repair factor IIH subunit TFB1
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 72.993328 KDa
SequenceString: MSHSGAAIFE KVSGIIAINE DVSPAELTWR STDGDKVHTV VLSTIDKLQA TPASSEKMML RLIGKVDESK KRKDNEGNEV VPKPQRHMF SFNNRTVMDN IKMTLQQIIS RYKDADIYEE KRRREESAQH TETPMSSSSV TAGTPTPHLD TPQLNNGAPL I NTAKLDDS ...String:
MSHSGAAIFE KVSGIIAINE DVSPAELTWR STDGDKVHTV VLSTIDKLQA TPASSEKMML RLIGKVDESK KRKDNEGNEV VPKPQRHMF SFNNRTVMDN IKMTLQQIIS RYKDADIYEE KRRREESAQH TETPMSSSSV TAGTPTPHLD TPQLNNGAPL I NTAKLDDS LSKEKLLTNL KLQQSLLKGN KVLMKVFQET VINAGLPPSE FWSTRIPLLR AFALSTSQKV GPYNVLSTIK PV ASSENKV NVNLSREKIL NIFENYPIVK KAYTDNVPKN FKEPEFWARF FSSKLFRKLR GEKIMQNDRG DVIIDRYLTL DQE FDRKDD DMLLHPVKKI IDLDGNIQDD PVVRGNRPDF TMQPGVDING NSDGTVDILK GMNRLSEKMI MALKNEYSRT NLQN KSNIT NDEEDEDNDE RNELKIDDLN ESYKTNYAII HLKRNAHEKT TDNDAKSSAD SIKNADLKVS NQQMLQQLSL VMDNL INKL DLNQVVPNNE VSNKINKRVI TAIKINAKQA KHNNVNSALG SFVDNTSQAN ELEVKSTLPI DLLESCRMLH TTCCEF LKH FYIHFQSGEQ KQASTVKKLY NHLKDCIEKL NELFQDVLNG DGESMSNTCT AYLKPVLNSI TLATHKYDEY FNEYNNN SN

+
Macromolecule #2: General transcription and DNA repair factor IIH subunit TFB4

MacromoleculeName: General transcription and DNA repair factor IIH subunit TFB4
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 37.506422 KDa
SequenceString: MDAISDPTFK HARSRKQVTE ESPSLLTVII EIAPKLWTTF DEEGNEKGSI IKVLEALIVF LNAHLAFNSA NKVAVIAAYS QGIKYLYPE STSALKASES ENKTRSDLKI INSDMYRRFR NVDETLVEEI YKLFELEKKQ IEQNSQRSTL AGAMSAGLTY V NRISKESV ...String:
MDAISDPTFK HARSRKQVTE ESPSLLTVII EIAPKLWTTF DEEGNEKGSI IKVLEALIVF LNAHLAFNSA NKVAVIAAYS QGIKYLYPE STSALKASES ENKTRSDLKI INSDMYRRFR NVDETLVEEI YKLFELEKKQ IEQNSQRSTL AGAMSAGLTY V NRISKESV TTSLKSRLLV LTCGSGSSKD EIFQYIPIMN CIFSATKMKC PIDVVKIGGS KESTFLQQTT DATNGVYLHV ES TEGLIQY LATAMFIDPS LRPIIVKPNH GSVDFRTSCY LTGRVVAVGF ICSVCLCVLS IIPPGNKCPA CDSQFDEHVI AKL KRKPVV PRLKAKKKVT KP

+
Macromolecule #3: DNA repair helicase RAD25

MacromoleculeName: DNA repair helicase RAD25 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 95.461664 KDa
SequenceString: MTDVEGYQPK SKGKIFPDMG ESFFSSDEDS PATDAEIDEN YDDNRETSEG RGERDTGAMV TGLKKPRKKT KSSRHTAADS SMNQMDAKD KALLQDTNSD IPADFVPDSV SGMFRSHDFS YLRLRPDHAS RPLWISPSDG RIILESFSPL AEQAQDFLVT I AEPISRPS ...String:
MTDVEGYQPK SKGKIFPDMG ESFFSSDEDS PATDAEIDEN YDDNRETSEG RGERDTGAMV TGLKKPRKKT KSSRHTAADS SMNQMDAKD KALLQDTNSD IPADFVPDSV SGMFRSHDFS YLRLRPDHAS RPLWISPSDG RIILESFSPL AEQAQDFLVT I AEPISRPS HIHEYKITAY SLYAAVSVGL ETDDIISVLD RLSKVPVAES IINFIKGATI SYGKVKLVIK HNRYFVETTQ AD ILQMLLN DSVIGPLRID SDHQVQPPED VLQQQLQQTA GKPATNVNPN DVEAVFSAVI GGDNEREEED DDIDAVHSFE IAN ESVEVV KKRCQEIDYP VLEEYDFRND HRNPDLDIDL KPSTQIRPYQ EKSLSKMFGN GRARSGIIVL PCGAGKTLVG ITAA CTIKK SVIVLCTSSV SVMQWRQQFL QWCTLQPENC AVFTSDNKEM FQTESGLVVS TYSMVANTRN RSHDSQKVMD FLTGR EWGF IILDEVHVVP AAMFRRVVST IAAHAKLGLT ATLVREDDKI GDLNFLIGPK LYEANWMELS QKGHIANVQC AEVWCP MTA EFYQEYLRET ARKRMLLYIM NPTKFQACQF LIQYHERRGD KIIVFSDNVY ALQEYALKMG KPFIYGSTPQ QERMNIL QN FQYNDQINTI FLSKVGDTSI DLPEATCLIQ ISSHYGSRRQ EAQRLGRILR AKRRNDEGFN AFFYSLVSKD TQEMYYST K RQAFLVDQGY AFKVITHLHG MENIPNLAYA SPRERRELLQ EVLLKNEEAA GIEVGDDADN SVGRGSNGHK RFKSKAVRG EGSLSGLAGG EDMAYMEYST NKNKELKEHH PLIRKMYYKN LKK

+
Macromolecule #4: RNA polymerase II transcription factor B subunit 5

MacromoleculeName: RNA polymerase II transcription factor B subunit 5 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 8.24349 KDa
SequenceString:
MARARKGALV QCDPSIKALI LQIDAKMSDI VLEELDDTHL LVNPSKVEFV KHELNRLLSK NIYNPMDEEE NQ

+
Macromolecule #5: General transcription and DNA repair factor IIH subunit TFB2

MacromoleculeName: General transcription and DNA repair factor IIH subunit TFB2
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 58.602312 KDa
SequenceString: MSDYSLKHSV TQYLEEIPQQ VQNRLYTSPA TCLAIYRILP PLAKFFIMAM VFNENEVPLL DLDKWVNSNG KLQFQNAIKS MKSLHLLIP NKSSGTLMIN LNPTFKISLR NALTGGEVQN SFGVVVEENV VSLDLLDEYS ANKWETILHF MVGTPLAKIP S EKVLNLLK ...String:
MSDYSLKHSV TQYLEEIPQQ VQNRLYTSPA TCLAIYRILP PLAKFFIMAM VFNENEVPLL DLDKWVNSNG KLQFQNAIKS MKSLHLLIP NKSSGTLMIN LNPTFKISLR NALTGGEVQN SFGVVVEENV VSLDLLDEYS ANKWETILHF MVGTPLAKIP S EKVLNLLK HSKLMEEVNS TGEFKITNEG FQFLLQEINS QLWTLLLQYL KMIETSKMDL VDVLHFIFML GALEVGKAYK ID ALSETQR IMLQDMRDYG LVFQKHSNDS IFYPTKLALM LTSDTKTIRS ASNAMDSVLR QNREEPSVNE DGANGKSTTD ITT SDDLNK AGLKNQDIPD GSLIVETNFK IYSYSNSPLQ IAVLSLFVHL KARFVNMVLG QITRESIRRA LTNGITADQI IAYL ETHAH PQMRRLAEEK LEKKLELDPN CKEPLQVLPP TVVDQIRLWQ LELDRVITYE GSLYSDFETS QEYNLLSKYA QDIGV LLWK DDKKKKFFIS KEGNSQVLDF AKRKLKKKQ

+
Macromolecule #6: DNA repair helicase RAD3

MacromoleculeName: DNA repair helicase RAD3 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 89.899047 KDa
SequenceString: MKFYIDDLPV LFPYPKIYPE QYNYMCDIKK TLDVGGNSIL EMPSGTGKTV SLLSLTIAYQ MHYPEHRKII YCSRTMSEIE KALVELENL MDYRTKELGY QEDFRGLGLT SRKNLCLHPE VSKERKGTVV DEKCRRMTNG QAKRKLEEDP EANVELCEYH E NLYNIEVE ...String:
MKFYIDDLPV LFPYPKIYPE QYNYMCDIKK TLDVGGNSIL EMPSGTGKTV SLLSLTIAYQ MHYPEHRKII YCSRTMSEIE KALVELENL MDYRTKELGY QEDFRGLGLT SRKNLCLHPE VSKERKGTVV DEKCRRMTNG QAKRKLEEDP EANVELCEYH E NLYNIEVE DYLPKGVFSF EKLLKYCEEK TLCPYFIVRR MISLCNIIIY SYHYLLDPKI AERVSNEVSK DSIVIFDEAH NI DNVCIES LSLDLTTDAL RRATRGANAL DERISEVRKV DSQKLQDEYE KLVQGLHSAD ILTDQEEPFV ETPVLPQDLL TEA IPGNIR RAEHFVSFLK RLIEYLKTRM KVLHVISETP KSFLQHLKQL TFIERKPLRF CSERLSLLVR TLEVTEVEDF TALK DIATF ATLISTYEEG FLLIIEPYEI ENAAVPNPIM RFTCLDASIA IKPVFERFSS VIITSGTISP LDMYPRMLNF KTVLQ KSYA MTLAKKSFLP MIITKGSDQV AISSRFEIRN DPSIVRNYGS MLVEFAKITP DGMVVFFPSY LYMESIVSMW QTMGIL DEV WKHKLILVET PDAQETSLAL ETYRKACSNG RGAILLSVAR GKVSEGIDFD HQYGRTVLMI GIPFQYTESR ILKARLE FM RENYRIREND FLSFDAMRHA AQCLGRVLRG KDDYGVMVLA DRRFSRKRSQ LPKWIAQGLS DADLNLSTDM AISNTKQF L RTMAQPTDPK DQEGVSVWSY EDLIKHQNSR KDQGGFIENE NKEGEQDEDE DEDIEMQ

+
Macromolecule #7: General transcription and DNA repair factor IIH subunit SSL1

MacromoleculeName: General transcription and DNA repair factor IIH subunit SSL1
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 52.370035 KDa
SequenceString: MAPVVISESE EDEDRVAITR RTKRQVHFDG EGDDRVDQQQ QQHSSSHRDR DKHVQRKKKK RLSNRNLQGS NGGYAWEDEI KRSWDLVKV DDEGDMASLV ASIVEARKKR TAKKNITPYQ RGIIRSLILT LDCSEAMLEK DLRPNRHAMI IQYAIDFVHE F FDQNPISQ ...String:
MAPVVISESE EDEDRVAITR RTKRQVHFDG EGDDRVDQQQ QQHSSSHRDR DKHVQRKKKK RLSNRNLQGS NGGYAWEDEI KRSWDLVKV DDEGDMASLV ASIVEARKKR TAKKNITPYQ RGIIRSLILT LDCSEAMLEK DLRPNRHAMI IQYAIDFVHE F FDQNPISQ MGIIIMRNGL AQLVSQVSGN PQDHIDALKS IRKQEPKGNP SLQNALEMAR GLLLPVPAHC TREVLIVFGS LS TTDPGDI HQTIDSLVSE KIRVKVLGLS AQVAICKELC KATNYGDESF YKILLDETHL KELFNEAVTP LPVNKINKGF TLV KMGFPT RIFEDTPTFC SCHSKLVYGG YFCPNCHSKV CSLPTVCPCC DLMLILSTHL ARSYHHLMPL KTFAEVPTTE KFRS EDCFS CQSRFPILKN HKNGKLLTSS RYRCEDCKQE FCVDCDVFIH EILHNCPGCE SKPVIT

+
Macromolecule #8: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 8 / Number of copies: 5 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

+
Macromolecule #9: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 9 / Number of copies: 1 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.6
Component:
ConcentrationName
20.0 mMHEPES
150.0 mMPotassium Acetate
5.0 mMDTT

Details: Sample dialyzed for 30 minutes into above buffer prior to grid making
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Details: Pelco easyGLOW glow discharge apparatus
VitrificationCryogen name: ETHANE / Instrument: LEICA EM CPC
Details: Grids were manually blotted for 2-3 seconds prior to plunge freezing.
DetailsSample was prepared by Grafix. Sample was monodispersed and well behaved by visual inspection

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000
Specialist opticsEnergy filter - Name: GIF Bioquantum
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
DetailsImages collected with image shift
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 6223 / Average exposure time: 2.6 sec. / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Particle selectionNumber selected: 1159858
Details: Particles picked by elliptical blob picking in cryoSPARC
CTF correctionSoftware - Name: CTFFIND (ver. 4.13)
Startup modelType of model: NONE
Details: De novo initial model obtained by SGD in cryoSPARC and RELION
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0.8)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0.8)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION
Details: Final reconstruction performed in RELION. Map locally filtered to FSC=0.5 by blocres
Number images used: 56101
DetailsCamera operated in super resolution mode.
FSC plot (resolution estimation)

-
Atomic model buiding 1

Initial model(PDB ID:

5oqj

,

6nmi

)
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-7k01:
Structure of TFIIH in TFIIH/Rad4-Rad23-Rad33 DNA opening complex

+
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://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