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- EMDB-21138: Mono-ubiquitinated Fanconi Anemia ID complex bound to ICL DNA -

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Basic information

Entry
Database: EMDB / ID: EMD-21138
TitleMono-ubiquitinated Fanconi Anemia ID complex bound to ICL DNA
Map dataconsensus reconstruction
Sample
  • Complex: Mono-ubiquitinated Fanconi Anemia ID complex bound to DNA
    • Protein or peptide: Fanconi anemia, complementation group I
    • Protein or peptide: Fanconi anemia group D2 protein
    • Protein or peptide: Ubiquitin
    • DNA: DNA (29-MER)
    • DNA: DNA (29-MER)
Function / homology
Function and homology information


regulation of CD40 signaling pathway / regulation of regulatory T cell differentiation / homologous chromosome pairing at meiosis / double-strand break repair involved in meiotic recombination / gamete generation / neuronal stem cell population maintenance / brain morphogenesis / DNA repair complex / mitotic intra-S DNA damage checkpoint signaling / interstrand cross-link repair ...regulation of CD40 signaling pathway / regulation of regulatory T cell differentiation / homologous chromosome pairing at meiosis / double-strand break repair involved in meiotic recombination / gamete generation / neuronal stem cell population maintenance / brain morphogenesis / DNA repair complex / mitotic intra-S DNA damage checkpoint signaling / interstrand cross-link repair / DNA polymerase binding / condensed chromosome / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Glycogen synthesis / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / TICAM1,TRAF6-dependent induction of TAK1 complex / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Negative regulation of FLT3 / Constitutive Signaling by NOTCH1 HD Domain Mutants / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / TICAM1-dependent activation of IRF3/IRF7 / NOTCH2 Activation and Transmission of Signal to the Nucleus / Regulation of FZD by ubiquitination / APC/C:Cdc20 mediated degradation of Cyclin B / p75NTR recruits signalling complexes / VLDLR internalisation and degradation / Downregulation of ERBB4 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / APC-Cdc20 mediated degradation of Nek2A / Regulation of innate immune responses to cytosolic DNA / InlA-mediated entry of Listeria monocytogenes into host cells / NF-kB is activated and signals survival / Regulation of pyruvate metabolism / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Pexophagy / Regulation of PTEN localization / Regulation of BACH1 activity / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by REV1 / TICAM1, RIP1-mediated IKK complex recruitment / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Translesion synthesis by POLK / Downregulation of TGF-beta receptor signaling / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLI / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Gap-filling DNA repair synthesis and ligation in GG-NER / IKK complex recruitment mediated by RIP1 / InlB-mediated entry of Listeria monocytogenes into host cell / Regulation of activated PAK-2p34 by proteasome mediated degradation / Josephin domain DUBs / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / positive regulation of protein ubiquitination / response to gamma radiation / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / Asymmetric localization of PCP proteins / NIK-->noncanonical NF-kB signaling / Regulation of NF-kappa B signaling / Ubiquitin-dependent degradation of Cyclin D / activated TAK1 mediates p38 MAPK activation / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Regulation of signaling by CBL / Vpu mediated degradation of CD4 / Negative regulators of DDX58/IFIH1 signaling / TP53 Regulates Transcription of DNA Repair Genes / NOTCH3 Activation and Transmission of Signal to the Nucleus / Assembly of the pre-replicative complex / Degradation of DVL / Deactivation of the beta-catenin transactivating complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Iron uptake and transport / Negative regulation of FGFR2 signaling / Negative regulation of FGFR3 signaling / Hh mutants are degraded by ERAD / Peroxisomal protein import
Similarity search - Function
Fanconi anemia group I protein / FANCI solenoid 1 cap / FANCI solenoid 1 domain / FANCI helical domain 1 / FANCI helical domain 2 / FANCI solenoid 3 domain / FANCI solenoid 4 domain / FANCI solenoid 2 domain / FANCI solenoid 1 cap / FANCI solenoid 1 ...Fanconi anemia group I protein / FANCI solenoid 1 cap / FANCI solenoid 1 domain / FANCI helical domain 1 / FANCI helical domain 2 / FANCI solenoid 3 domain / FANCI solenoid 4 domain / FANCI solenoid 2 domain / FANCI solenoid 1 cap / FANCI solenoid 1 / FANCI solenoid 2 / FANCI solenoid 3 / FANCI solenoid 4 / FANCI helical domain 1 / FANCI helical domain 2 / Fanconi anaemia protein FANCD2 / Fanconi anaemia protein FancD2 nuclease / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
Fanconi anemia, complementation group I / Polyubiquitin-C / Fanconi anemia group D2 protein / Fanconi anemia group I protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsPavletich NP
Funding support United States, 1 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Nature / Year: 2020
Title: DNA clamp function of the monoubiquitinated Fanconi anaemia ID complex.
Authors: Renjing Wang / Shengliu Wang / Ankita Dhar / Christopher Peralta / Nikola P Pavletich /
Abstract: The ID complex, involving the proteins FANCI and FANCD2, is required for the repair of DNA interstrand crosslinks (ICL) and related lesions. These proteins are mutated in Fanconi anaemia, a disease ...The ID complex, involving the proteins FANCI and FANCD2, is required for the repair of DNA interstrand crosslinks (ICL) and related lesions. These proteins are mutated in Fanconi anaemia, a disease in which patients are predisposed to cancer. The Fanconi anaemia pathway of ICL repair is activated when a replication fork stalls at an ICL; this triggers monoubiquitination of the ID complex, in which one ubiquitin molecule is conjugated to each of FANCI and FANCD2. Monoubiquitination of ID is essential for ICL repair by excision, translesion synthesis and homologous recombination; however, its function remains unknown. Here we report a cryo-electron microscopy structure of the monoubiquitinated human ID complex bound to DNA, and reveal that it forms a closed ring that encircles the DNA. By comparison with the structure of the non-ubiquitinated ID complex bound to ICL DNA-which we also report here-we show that monoubiquitination triggers a complete rearrangement of the open, trough-like ID structure through the ubiquitin of one protomer binding to the other protomer in a reciprocal fashion. These structures-together with biochemical data-indicate that the monoubiquitinated ID complex loses its preference for ICL and related branched DNA structures, and becomes a sliding DNA clamp that can coordinate the subsequent repair reactions. Our findings also reveal how monoubiquitination in general can induce an alternative protein structure with a new function.
History
DepositionDec 17, 2019-
Header (metadata) releaseFeb 5, 2020-
Map releaseMar 18, 2020-
UpdateNov 25, 2020-
Current statusNov 25, 2020Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6vae
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21138.png

Downloads & links

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Map

FileDownload / File: emd_21138.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationconsensus reconstruction
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 256 pix.
= 278.648 Å		1.09 Å/pix.
x 256 pix.
= 278.648 Å		1.09 Å/pix.
x 256 pix.
= 278.648 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08847 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.012 / Movie #1: 0.015
Minimum - Maximum-0.11674949 - 0.20537838
Average (Standard dev.)0.00000294707 (±0.0038885586)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 278.64832 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.088468751.088468751.08846875
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z278.648278.648278.648
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ400400400
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.1170.2050.000

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Supplemental data

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Additional map: refmac composite map

Fileemd_21138_additional_1.map
Annotationrefmac composite map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: focus3 map

Fileemd_21138_additional_2.map
Annotationfocus3 map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: focus2 map

Fileemd_21138_additional_3.map
Annotationfocus2 map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: focus1 map

Fileemd_21138_additional_4.map
Annotationfocus1 map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Mono-ubiquitinated Fanconi Anemia ID complex bound to DNA

EntireName: Mono-ubiquitinated Fanconi Anemia ID complex bound to DNA
Components
  • Complex: Mono-ubiquitinated Fanconi Anemia ID complex bound to DNA
    • Protein or peptide: Fanconi anemia, complementation group I
    • Protein or peptide: Fanconi anemia group D2 protein
    • Protein or peptide: Ubiquitin
    • DNA: DNA (29-MER)
    • DNA: DNA (29-MER)

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Supramolecule #1: Mono-ubiquitinated Fanconi Anemia ID complex bound to DNA

SupramoleculeName: Mono-ubiquitinated Fanconi Anemia ID complex bound to DNA
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Fanconi anemia, complementation group I

MacromoleculeName: Fanconi anemia, complementation group I / type: protein_or_peptide / ID: 1
Details: isopeptide bond between Lys523 Nz and the C-terminus of ubiquitin (chain C)
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 149.566047 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI FKGSPCSEEA GTLRRRKIYT CCIQLVESGD LQKEIVSEI IGLLMLEAHH FPGPLLVELA NEFISAVREG SLVNGKSLEL LPIILTVLAT KKENLAYGKG VLSGEECKKQ L INTLCSGR ...String:
MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI FKGSPCSEEA GTLRRRKIYT CCIQLVESGD LQKEIVSEI IGLLMLEAHH FPGPLLVELA NEFISAVREG SLVNGKSLEL LPIILTVLAT KKENLAYGKG VLSGEECKKQ L INTLCSGR WDQQYVIQLT SMFKDVPLTA EEVEFVVEKA LSMFSKMNLQ EIPPLVYQLL VLSSKGSRKS VLEGIIAFFS AL DKQHNEE QSGDELLDVV TVPSGELRHV EGTIILHIVF AIKLDYELGR ELVKHLKVGQ QGDSNNNLSP FSIALLLSVT RIQ RFQDQV LDLLKTSVVK SFKDLQLLQG SKFLQNLVPH RSYVSTMILE VVKNSVHSWD HVTQGLVELG FILMDSYGPK KVLD GKTIE TSPSLSRMPN QHACKLGANI LLETFKIHEM IRQEILEQVL NRVVTRASSP ISHFLDLLSN IVMYAPLVLQ NCSSK VTEA FDYLSFLPLQ TVQRLLKAVQ PLLKVSMSMR DCLILVLRKA MFANQLDARK SAVAGFLLLL KNFKVLGSLS SSQCSQ SLS VSQVHVDVHS HYNSVANETF CLEIMDSLRR CLSQQADVRL MLYEGFYDVL RRNSQLANSV MQTLLSQLKQ FYEPEPD LL PPLKLEACIL TQGDQISLQE PLDYLLCCIQ HCLAWYKNTV IPLQQGEEEE EEEEAFYEDL DDILESITNR MIKSELED F ELDKSADFSQ STSIGIKNNI SAFLVMGVCE VLIEYNFSIS SFSKNRFEDI LSLFMCYKKL SDILNEKAGK AKTKMANKT SDSLLSMKFV SSLLTALFRD SIQSHQESLS VLRSSNEFMR YAVNVALQKV QQLKETGHVS GPDGQNPEKI FQNLCDLTRV LLWRYTSIP TSVEESGKKE KGKSISLLCL EGLQKIFSAV QQFYQPKIQQ FLRALDVTDK EGEEREDADV SVTQRTAFQI R QFQRSLLN LLSSQEEDFN SKEALLLVTV LTSLSKLLEP SSPQFVQMLS WTSKICKENS REDALFCKSL MNLLFSLHVS YK SPVILLR DLSQDIHGHL GDIDQDVEVE KTNHFAIVNL RTAAPTVCLL VLSQAEKVLE EVDWLITKLK GQVSQETLSE EAS SQATLP NQPVEKAIIM QLGTLLTFFH ELVQTALPSG SCVDTLLKDL CKMYTTLTAL VRYYLQVCQS SGGIPKNMEK LVKL SGSHL TPLCYSFISY VQNKSKSLNY TGEKKEKPAV VATAMARVLR ETKPIPNLIF AIEQYEKFLI HLSKKSKVSL MQHMK LSTS RDFKIKGNIL DMVLREDGED ENEEGTASEH GGQNKEPAKK KRKK

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Macromolecule #2: Fanconi anemia group D2 protein

MacromoleculeName: Fanconi anemia group D2 protein / type: protein_or_peptide / ID: 2
Details: isopeptide bond between Lys561 Nz and the C-terminus of ubiquitin (chain D)
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 164.314516 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MVSKRRLSKS EDKESLTEDA SKTRKQPLSK KTKKSHIANE VEENDSIFVK LLKISGIILK TGESQNQLAV DQIAFQKKLF QTLRRHPSY PKIIEEFVSG LESYIEDEDS FRNCLLSCER LQDEEASMGA SYSKSLIKLL LGIDILQPAI IKTLFEKLPE Y FFENKNSD ...String:
MVSKRRLSKS EDKESLTEDA SKTRKQPLSK KTKKSHIANE VEENDSIFVK LLKISGIILK TGESQNQLAV DQIAFQKKLF QTLRRHPSY PKIIEEFVSG LESYIEDEDS FRNCLLSCER LQDEEASMGA SYSKSLIKLL LGIDILQPAI IKTLFEKLPE Y FFENKNSD EINIPRLIVS QLKWLDRVVD GKDLTTKIMQ LISIAPENLQ HDIITSLPEI LGDSQHADVG KELSDLLIEN TS LTVPILD VLSSLRLDPN FLLKVRQLVM DKLSSIRLED LPVIIKFILH SVTAMDTLEV ISELREKLDL QHCVLPSRLQ ASQ VKLKSK GRASSSGNQE SSGQSCIILL FDVIKSAIRY EKTISEAWIK AIENTASVSE HKVFDLVMLF IIYSTNTQTK KYID RVLRN KIRSGCIQEQ LLQSTFSVHY LVLKDMCSSI LSLAQSLLHS LDQSIISFGS LLYKYAFKFF DTYCQQEVVG ALVTH ICSG NEAEVDTALD VLLELVVLNP SAMMMNAVFV KGILDYLDNI SPQQIRKLFY VLSTLAFSKQ NEASSHIQDD MHLVIR KQL SSTVFKYKLI GIIGAVTMAG IMAADRSESP SLTQERANLS DEQCTQVTSL LQLVHSCSEQ SPQASALYYD EFANLIQ HE KLDPKALEWV GQTICNDFQD AFVVDSCVVP EGDFPFPVKA LYGLEEYDTQ NGIAINLLPL LFSQDFAKDG GPVTSQES G QKLVSPLCLA PYFRLLRLCV ERQHNGNLEE IDGLLDCPIF LTDLEPGEKL ESMSAKERSF MCSLIFLTLN WFREIVNAF CQETSPEMKG KVLTRLKHIV ELQIILEKYL AVTPDYVPPL GNFDVETLDI TPHTVTAISA KIRKKGKIER KQKTDGSKTS SSDTLSEEK NSECDPTPSH RGQLNKEFTG KEEKTSLLLH NSHAFFRELD IEVFSILHCG LVTKFILDTE MHTEATEVVQ L GPPELLFL LEDLSQKLES MLTPPIARRV PFLKNKGSRN IGFSHLQQRS AQEIVHCVFQ LLTPMCNHLE NIHNYFQCLA AE NHGVVDG PGVKVQEYHI MSSCYQRLLQ IFHGLFAWSG FSQPENQNLL YSALHVLSSR LKQGEHSQPL EELLSQSVHY LQN FHQSIP SFQCALYLIR LLMVILEKST ASAQNKEKIA SLARQFLCRV WPSGDKEKSN ISNDQLHALL CIYLEHTESI LKAI EEIAG VGVPELINSP KDASSSTFPT LTRHTFVVFF RVMMAELEKT VKKIEPGTAA DSQQIHEEKL LYWNMAVRDF SILIN LIKV FDSHPVLHVC LKYGRLFVEA FLKQCMPLLD FSFRKHREDV LSLLETFQLD TRLLHHLCGH SKIHQDTRLT QHVPLL KKT LELLVCRVKA MLTLNNCREA FWLGNLKNRD LQGEEIKSQN SQESTADESE DDMSSQASKS KATEDGEEDE VSAGEKE QD SDESYDDSD

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Macromolecule #3: Ubiquitin

MacromoleculeName: Ubiquitin / type: protein_or_peptide / ID: 3
Details: isopeptide bond between C-terminus of ubiquitin (chain C) and Lys523 Nz of FANCI (chain A); isopeptide bond between C-terminus of ubiquitin (chain D) and Lys561 Nz of FANCD2 (chain B)
Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.576831 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG

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Macromolecule #4: DNA (29-MER)

MacromoleculeName: DNA (29-MER) / type: dna / ID: 4 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.951746 KDa
SequenceString:
(DG)(DG)(DC)(DA)(DC)(DA)(DG)(DG)(DT)(DT) (DC)(DA)(DG)(DA)(DG)(DC)(DA)(DG)(DG)(DC) (DG)(DT)(DT)(DC)(DC)(DG)(DT)(DT)(DC)

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Macromolecule #5: DNA (29-MER)

MacromoleculeName: DNA (29-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.880711 KDa
SequenceString:
(DG)(DA)(DA)(DC)(DG)(DG)(DA)(DA)(DC)(DG) (DC)(DC)(DT)(DG)(DC)(DT)(DC)(DT)(DG)(DA) (DA)(DC)(DC)(DT)(DG)(DT)(DG)(DC)(DC)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
GridDetails: unspecified
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 51.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: CTFFIND (ver. 4)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 301158
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3)
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

Initial modelPDB ID:

3s4w

RefinementSpace: RECIPROCAL / Protocol: OTHER / Overall B value: 150 / Target criteria: R-factor
Output model

PDB-6vae:
Mono-ubiquitinated Fanconi Anemia ID complex bound to ICL DNA

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