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- EMDB-21139: Structure of mono-ubiquitinated FANCD2 bound to non-ubiquitinated... -

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Basic information

Entry
Database: EMDB / ID: EMD-21139
TitleStructure of mono-ubiquitinated FANCD2 bound to non-ubiquitinated FANCI and to DNA.
Map dataconsensus reconstruction
Sample
  • Complex: Mono-ubiquitinated FANCD2 bound to non-ubiquitinated FANCI and 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)
KeywordsDNA clamp / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex
Function / homology
Function and homology information


regulation of CD40 signaling pathway / double-strand break repair involved in meiotic recombination / gamete generation / homologous chromosome pairing at meiosis / regulation of regulatory T cell differentiation / neuronal stem cell population maintenance / brain morphogenesis / mitotic intra-S DNA damage checkpoint signaling / DNA repair complex / Maturation of protein E ...regulation of CD40 signaling pathway / double-strand break repair involved in meiotic recombination / gamete generation / homologous chromosome pairing at meiosis / regulation of regulatory T cell differentiation / neuronal stem cell population maintenance / brain morphogenesis / mitotic intra-S DNA damage checkpoint signaling / DNA repair complex / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Constitutive Signaling by NOTCH1 HD Domain Mutants / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / interstrand cross-link repair / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / InlA-mediated entry of Listeria monocytogenes into host cells / Regulation of pyruvate metabolism / TRAF6-mediated induction of TAK1 complex within TLR4 complex / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Pexophagy / VLDLR internalisation and degradation / Regulation of PTEN localization / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / condensed chromosome / Translesion synthesis by REV1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / InlB-mediated entry of Listeria monocytogenes into host cell / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / DNA polymerase binding / TICAM1, RIP1-mediated IKK complex recruitment / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / positive regulation of protein ubiquitination / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / IKK complex recruitment mediated by RIP1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Regulation of activated PAK-2p34 by proteasome mediated degradation / TNFR1-induced NF-kappa-B signaling pathway / PINK1-PRKN Mediated Mitophagy / TCF dependent signaling in response to WNT / Autodegradation of Cdh1 by Cdh1:APC/C / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / APC/C:Cdc20 mediated degradation of Securin / activated TAK1 mediates p38 MAPK activation / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / Regulation of signaling by CBL / NIK-->noncanonical NF-kB signaling / NOTCH3 Activation and Transmission of Signal to the Nucleus / SCF-beta-TrCP mediated degradation of Emi1 / Negative regulators of DDX58/IFIH1 signaling / Deactivation of the beta-catenin transactivating complex / TNFR2 non-canonical NF-kB pathway / Negative regulation of FGFR3 signaling / AUF1 (hnRNP D0) binds and destabilizes mRNA / Fanconi Anemia Pathway / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Negative regulation of FGFR2 signaling / Degradation of DVL / Peroxisomal protein import / Negative regulation of FGFR4 signaling / Stabilization of p53 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Negative regulation of FGFR1 signaling / EGFR downregulation
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 / Ubiquitin domain signature. / Ubiquitin conserved site / 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: 3.9 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) releaseJan 15, 2020-
Map releaseMar 18, 2020-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.012
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.012
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6vaf
  • Surface level: 0.012
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21139.png

Downloads & links

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Map

FileDownload / File: emd_21139.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: 0.012
Minimum - Maximum-0.05155352 - 0.09800101
Average (Standard dev.)0.0000012192612 (±0.002962743)
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-0.0520.0980.000

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Supplemental data

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Additional map: focus1 map

Fileemd_21139_additional_1.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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Additional map: focus2 map

Fileemd_21139_additional_2.map
Annotationfocus2 map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: focus3 map

Fileemd_21139_additional_3.map
Annotationfocus3 map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: refmac composite map

Fileemd_21139_additional_4.map
Annotationrefmac composite 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 FANCD2 bound to non-ubiquitinated FANCI and to DNA

EntireName: Mono-ubiquitinated FANCD2 bound to non-ubiquitinated FANCI and to DNA
Components
  • Complex: Mono-ubiquitinated FANCD2 bound to non-ubiquitinated FANCI and 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 FANCD2 bound to non-ubiquitinated FANCI and to DNA

SupramoleculeName: Mono-ubiquitinated FANCD2 bound to non-ubiquitinated FANCI and 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 / 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

UniProtKB: Fanconi anemia, complementation group I

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Macromolecule #2: Fanconi anemia group D2 protein

MacromoleculeName: Fanconi anemia group D2 protein / type: protein_or_peptide / ID: 2 / 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

UniProtKB: Fanconi anemia group D2 protein

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Macromolecule #3: Ubiquitin

MacromoleculeName: Ubiquitin / type: protein_or_peptide / ID: 3 / Number of copies: 1 / 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

UniProtKB: Polyubiquitin-C

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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

Startup modelType of model: PDB ENTRY
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 57993
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


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: RECIPROCAL / Protocol: OTHER / Overall B value: 195 / Target criteria: R-factor
Output model

PDB-6vaf:
Structure of mono-ubiquitinated FANCD2 bound to non-ubiquitinated FANCI and to DNA

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