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- EMDB-31742: Structure of the Dicer-2-R2D2 heterodimer bound to small RNA duplex -

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Basic information

Entry
Database: EMDB / ID: EMD-31742
TitleStructure of the Dicer-2-R2D2 heterodimer bound to small RNA duplex
Map data
Sample
  • Complex: Dicer-2-R2D2-siRNA
    • Protein or peptide: Dicer-2, isoform A
    • Protein or peptide: R2D2
    • RNA: RNA (5'-R(P*UP*GP*AP*GP*G)-3')
    • RNA: RNA (5'-R(P*CP*CP*UP*CP*UP*CP*U)-3')
    • RNA: RNA (5'-R(*AP*UP*GP*AP*GP*GP*UP*AP*GP*UP*AP*GP*GP*UP*UP*GP*UP*AP*UP*AP*G)-3')
    • RNA: RNA (5'-R(*CP*UP*AP*UP*AP*CP*AP*AP*CP*CP*UP*AP*CP*UP*AP*CP*CP*UP*CP*UP*C)-3')
Function / homology
Function and homology information


follicle cell of egg chamber stalk formation / regulatory ncRNA processing / bidentate ribonuclease III activity / positive regulation of Toll signaling pathway / MicroRNA (miRNA) biogenesis / Small interfering RNA (siRNA) biogenesis / PKR-mediated signaling / dsRNA transport / regulation of regulatory ncRNA processing / dosage compensation by hyperactivation of X chromosome ...follicle cell of egg chamber stalk formation / regulatory ncRNA processing / bidentate ribonuclease III activity / positive regulation of Toll signaling pathway / MicroRNA (miRNA) biogenesis / Small interfering RNA (siRNA) biogenesis / PKR-mediated signaling / dsRNA transport / regulation of regulatory ncRNA processing / dosage compensation by hyperactivation of X chromosome / global gene silencing by mRNA cleavage / ribonuclease III / deoxyribonuclease I activity / apoptotic DNA fragmentation / detection of virus / RISC-loading complex / regulatory ncRNA-mediated post-transcriptional gene silencing / RISC complex assembly / ribonuclease III activity / siRNA processing / siRNA binding / ATP-dependent activity, acting on RNA / positive regulation of innate immune response / RISC complex / heterochromatin formation / positive regulation of defense response to virus by host / locomotory behavior / mRNA 3'-UTR binding / helicase activity / cytoplasmic ribonucleoprotein granule / cellular response to virus / double-stranded RNA binding / defense response to virus / perinuclear region of cytoplasm / ATP hydrolysis activity / RNA binding / ATP binding / nucleus / cytoplasm
Similarity search - Function
: / Dicer, platform domain / Dicer dimerisation domain / Dicer dimerisation domain / Dicer dimerisation domain superfamily / Dicer double-stranded RNA-binding fold domain profile. / Ribonuclease III domain / Ribonuclease III family domain profile. / Ribonuclease III family / Ribonuclease III domain ...: / Dicer, platform domain / Dicer dimerisation domain / Dicer dimerisation domain / Dicer dimerisation domain superfamily / Dicer double-stranded RNA-binding fold domain profile. / Ribonuclease III domain / Ribonuclease III family domain profile. / Ribonuclease III family / Ribonuclease III domain / PAZ / PAZ domain / PAZ domain / PAZ domain profile. / Double-stranded RNA binding motif / Double-stranded RNA binding motif / Ribonuclease III, endonuclease domain superfamily / Double stranded RNA-binding domain (dsRBD) profile. / Double-stranded RNA-binding domain / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Helicase conserved C-terminal domain / 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 / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Endoribonuclease Dcr-2 / LD06392p
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsYamaguchi S / Nishizawa T / Kusakizako T / Yamashita K / Tomita A / Hirano H / Nishimasu H / Nureki O
Funding support Japan, 1 items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)202111067 Japan
CitationJournal: Nature / Year: 2022
Title: Structure of the Dicer-2-R2D2 heterodimer bound to a small RNA duplex.
Authors: Sonomi Yamaguchi / Masahiro Naganuma / Tomohiro Nishizawa / Tsukasa Kusakizako / Yukihide Tomari / Hiroshi Nishimasu / Osamu Nureki /
Abstract: In flies, Argonaute2 (Ago2) and small interfering RNA (siRNA) form an RNA-induced silencing complex to repress viral transcripts. The RNase III enzyme Dicer-2 associates with its partner protein R2D2 ...In flies, Argonaute2 (Ago2) and small interfering RNA (siRNA) form an RNA-induced silencing complex to repress viral transcripts. The RNase III enzyme Dicer-2 associates with its partner protein R2D2 and cleaves long double-stranded RNAs to produce 21-nucleotide siRNA duplexes, which are then loaded into Ago2 in a defined orientation. Here we report cryo-electron microscopy structures of the Dicer-2-R2D2 and Dicer-2-R2D2-siRNA complexes. R2D2 interacts with the helicase domain and the central linker of Dicer-2 to inhibit the promiscuous processing of microRNA precursors by Dicer-2. Notably, our structure represents the strand-selection state in the siRNA-loading process, and reveals that R2D2 asymmetrically recognizes the end of the siRNA duplex with the higher base-pairing stability, and the other end is exposed to the solvent and is accessible by Ago2. Our findings explain how R2D2 senses the thermodynamic asymmetry of the siRNA and facilitates the siRNA loading into Ago2 in a defined orientation, thereby determining which strand of the siRNA duplex is used by Ago2 as the guide strand for target silencing.
History
DepositionAug 20, 2021-
Header (metadata) releaseMar 23, 2022-
Map releaseMar 23, 2022-
UpdateJul 27, 2022-
Current statusJul 27, 2022Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_31742.png

Downloads & links

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Map

FileDownload / File: emd_31742.map.gz / Format: CCP4 / Size: 36.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.9985 Å
Density
Contour LevelBy AUTHOR: 0.0208
Minimum - Maximum-0.069547065 - 0.12095462
Average (Standard dev.)0.00032967346 (±0.0041563446)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions212212212
Spacing212212212
CellA=B=C: 211.68117 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_31742_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_31742_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_31742_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram (log scale)

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Sample components

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Entire : Dicer-2-R2D2-siRNA

EntireName: Dicer-2-R2D2-siRNA
Components
  • Complex: Dicer-2-R2D2-siRNA
    • Protein or peptide: Dicer-2, isoform A
    • Protein or peptide: R2D2
    • RNA: RNA (5'-R(P*UP*GP*AP*GP*G)-3')
    • RNA: RNA (5'-R(P*CP*CP*UP*CP*UP*CP*U)-3')
    • RNA: RNA (5'-R(*AP*UP*GP*AP*GP*GP*UP*AP*GP*UP*AP*GP*GP*UP*UP*GP*UP*AP*UP*AP*G)-3')
    • RNA: RNA (5'-R(*CP*UP*AP*UP*AP*CP*AP*AP*CP*CP*UP*AP*CP*UP*AP*CP*CP*UP*CP*UP*C)-3')

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Supramolecule #1: Dicer-2-R2D2-siRNA

SupramoleculeName: Dicer-2-R2D2-siRNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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Macromolecule #1: Dicer-2, isoform A

MacromoleculeName: Dicer-2, isoform A / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: deoxyribonuclease I
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Molecular weightTheoretical: 199.309 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: HHHHHHHHAA AMEDVEIKPR GYQLRLVDHL TKSNGIVYLP TGSGKTFVAI LVLKRFSQDF DKPIESGGKR ALFMCNTVEL ARQQAMAVR RCTNFKVGFY VGEQGVDDWT RGMWSDEIKK NQVLVGTAQV FLDMVTQTYV ALSSLSVVII DECHHGTGHH P FREFMRLF ...String:
HHHHHHHHAA AMEDVEIKPR GYQLRLVDHL TKSNGIVYLP TGSGKTFVAI LVLKRFSQDF DKPIESGGKR ALFMCNTVEL ARQQAMAVR RCTNFKVGFY VGEQGVDDWT RGMWSDEIKK NQVLVGTAQV FLDMVTQTYV ALSSLSVVII DECHHGTGHH P FREFMRLF TIANQTKLPR VVGLTGVLIK GNEITNVATK LKELEITYRG NIITVSDTKE LENVMLYATK PTEVMVSFPH QE QVLTVTR LISAEIEKFY VSLDLMNIGV QPIRRSKSLQ CLRDPSKKSF VKQLFNDFLY QMKEYGIYAA SIAIISLIVE FDI KRRQAE TLSVKLMHRT ALTLCEKIRH LLVQKLQDMT YDDDDDNVNT EEVIMNFSTP KVQRFLMSLK VSFADKDPKD ICCL VFVER RYTCKCIYGL LLNYIQSTPE LRNVLTPQFM VGRNNISPDF ESVLERKWQK SAIQQFRDGN ANLMICSSVL EEGID VQAC NHVFILDPVK TFNMYVQSKG RARTTEAKFV LFTADKEREK TIQQIYQYRK AHNDIAEYLK DRVLEKTEPE LYEIKG HFQ DDIDPFTNEN GAVLLPNNAL AILHRYCQTI PTDAFGFVIP WFHVLQEDER DRIFGVSAKG KHVISINMPV NCMLRDT IY SDPMDNVKTA KISAAFKACK VLYSLGELNE RFVPKTLKER VASIADVHFE HWNKYGDSVT ATVNKADKSK DRTYKTEC P LEFYDALPRV GEICYAYEIF LEPQFESCEY TEHMYLNLQT PRNYAILLRN KLPRLAEMPL FSNQGKLHVR VANAPLEVI IQNSEQLELL HQFHGMVFRD ILKIWHPFFV LDRRSKENSY LVVPLILGAG EQKCFDWELM TNFRRLPQSH GSNVQQREQQ PAPRPEDFE GKIVTQWYAN YDKPMLVTKV HRELTPLSYM EKNQQDKTYY EFTMSKYGNR IGDVVHKDKF MIEVRDLTEQ L TFYVHNRG KFNAKSKAKM KVILIPELCF NFNFPGDLWL KLIFLPSILN RMYFLLHAEA LRKRFNTYLN LHLLPFNGTD YM PRPLEID YSLKRNVDPL GNVIPTEDIE EPKSLLEPMP TKSIEASVAN LEITEFENPW QKYMEPVDLS RNLLSTYPVE LDY YYHFSV GNVCEMNEMD FEDKEYWAKN QFHMPTGNIY GNRTPAKTNA NVPALMPSKP TVRGKVKPLL ILQKTVSKEH ITPA EQGEF LAAITASSAA DVFDMERLEI LGDSFLKLSA TLYLASKYSD WNEGTLTEVK SKLVSNRNLL FCLIDADIPK TLNTI QFTP RYTWLPPGIS LPHNVLALWR ENPEFAKIIG PHNLRDLALG DEESLVKGNC SDINYNRFVE GCRANGQSFY AGADFS SEV NFCVGLVTIP NKVIADTLEA LLGVIVKNYG LQHAFKMLEY FKICRADIDK PLTQLLNLEL GGKKMRANVN TTEIDGF LI NHYYLEKNLG YTFKDRRYLL QALTHPSYPT NRITGSYQEL EFIGDAILDF LISAYIFENN TKMNPGALTD LRSALVNN T TLACICVRHR LHFFILAENA KLSEIISKFV NFQESQGHRV TNYVRILLEE ADVQPTPLDL DDELDMTELP HANKCISQE AEKGVPPKGE FNMSTNVDVP KALGDVLEAL IAAVYLDCRD LQRTWEVIFN LFEPELQEFT RKVPINHIRQ LVEHKHAKPV FSSPIVEGE TVMVSCQFTC MEKTIKVYGF GSNKDQAKLS AAKHALQQLS KCDA

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Macromolecule #2: R2D2

MacromoleculeName: R2D2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Molecular weightTheoretical: 39.920363 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDYKDHDGDY KDHDIDYKDD DDKHRYTSLY KKAGSAAAPF TMDNKSAVSA LQEFCARTQI NLPTYSFIPG EDGGYVCKVE LLEIEALGN GRSKRDAKHL AASNILRKIQ LLPGIHGLMK DSTVGDLDEE LTNLNRDMVK ELRDYCVRRE MPLPCIEVVQ Q SGTPSAPE ...String:
MDYKDHDGDY KDHDIDYKDD DDKHRYTSLY KKAGSAAAPF TMDNKSAVSA LQEFCARTQI NLPTYSFIPG EDGGYVCKVE LLEIEALGN GRSKRDAKHL AASNILRKIQ LLPGIHGLMK DSTVGDLDEE LTNLNRDMVK ELRDYCVRRE MPLPCIEVVQ Q SGTPSAPE FVACCSVASI VRYGKSDKKK DARQRAAIEM LALISSNSDN LRPDQMQVAS TSKLKVVDME ESMEELEALR RK KFTTYWE LKEAGSVDHT GMRLCDRHNY FKNFYPTLKK EAIEAINSDE YESSKDKAMD VMSSLKITPK ISEVESSSLV PLL SVELNC AFDVVLMAKE TDIYDHIIDY FRTMLI

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Macromolecule #3: RNA (5'-R(P*UP*GP*AP*GP*G)-3')

MacromoleculeName: RNA (5'-R(P*UP*GP*AP*GP*G)-3') / type: rna / ID: 3 / Number of copies: 1
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Molecular weightTheoretical: 6.812045 KDa
SequenceString:
UGAGGUAGUA GGUUGUAUAG U

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Macromolecule #4: RNA (5'-R(P*CP*CP*UP*CP*UP*CP*U)-3')

MacromoleculeName: RNA (5'-R(P*CP*CP*UP*CP*UP*CP*U)-3') / type: rna / ID: 4 / Number of copies: 1
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Molecular weightTheoretical: 6.514892 KDa
SequenceString:
UAUACAACCU ACUACCUCUC U

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Macromolecule #5: RNA (5'-R(*AP*UP*GP*AP*GP*GP*UP*AP*GP*UP*AP*GP*GP*UP*UP*GP*UP*AP*...

MacromoleculeName: RNA (5'-R(*AP*UP*GP*AP*GP*GP*UP*AP*GP*UP*AP*GP*GP*UP*UP*GP*UP*AP*UP*AP*G)-3')
type: rna / ID: 5 / Number of copies: 1
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Molecular weightTheoretical: 7.141251 KDa
SequenceString:
AUGAGGUAGU AGGUUGUAUA GU

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Macromolecule #6: RNA (5'-R(*CP*UP*AP*UP*AP*CP*AP*AP*CP*CP*UP*AP*CP*UP*AP*CP*CP*UP*...

MacromoleculeName: RNA (5'-R(*CP*UP*AP*UP*AP*CP*AP*AP*CP*CP*UP*AP*CP*UP*AP*CP*CP*UP*CP*UP*C)-3')
type: rna / ID: 6 / Number of copies: 1
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Molecular weightTheoretical: 6.820074 KDa
SequenceString:
CUAUACAACC UACUACCUCU CU

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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: 7.4
VitrificationCryogen name: NITROGEN

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 48.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 144979
FSC plot (resolution estimation)

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