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Open data
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Basic information
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Title | Human NEXT dimer - focused reconstruction of the single MTR4 | |||||||||||||||
![]() | NEXT_L_focused_on_MTR4_postprocess | |||||||||||||||
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![]() | HELICASE / ATPASE / RNA DEGRADATION / EXOSOME / RNA BINDING PROTEIN | |||||||||||||||
Function / homology | ![]() : / snRNA catabolic process / TRAMP complex / RNA catabolic process / maturation of 5.8S rRNA / Major pathway of rRNA processing in the nucleolus and cytosol / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / mRNA splicing, via spliceosome / rRNA processing ...: / snRNA catabolic process / TRAMP complex / RNA catabolic process / maturation of 5.8S rRNA / Major pathway of rRNA processing in the nucleolus and cytosol / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / mRNA splicing, via spliceosome / rRNA processing / RNA helicase activity / nuclear body / RNA helicase / nuclear speck / DNA damage response / nucleolus / ATP hydrolysis activity / RNA binding / zinc ion binding / nucleoplasm / ATP binding / nucleus Similarity search - Function | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||||||||
![]() | Gerlach P / Lingaraju M / Salerno-Kochan A / Bonneau F / Basquin J / Conti E | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome. Authors: Piotr Gerlach / William Garland / Mahesh Lingaraju / Anna Salerno-Kochan / Fabien Bonneau / Jérôme Basquin / Torben Heick Jensen / Elena Conti / ![]() ![]() Abstract: In mammalian cells, spurious transcription results in a vast repertoire of unproductive non-coding RNAs, whose deleterious accumulation is prevented by rapid decay. The nuclear exosome targeting ...In mammalian cells, spurious transcription results in a vast repertoire of unproductive non-coding RNAs, whose deleterious accumulation is prevented by rapid decay. The nuclear exosome targeting (NEXT) complex plays a central role in directing non-functional transcripts to exosome-mediated degradation, but the structural and molecular mechanisms remain enigmatic. Here, we elucidated the architecture of the human NEXT complex, showing that it exists as a dimer of MTR4-ZCCHC8-RBM7 heterotrimers. Dimerization preconfigures the major MTR4-binding region of ZCCHC8 and arranges the two MTR4 helicases opposite to each other, with each protomer able to function on many types of RNAs. In the inactive state of the complex, the 3' end of an RNA substrate is enclosed in the MTR4 helicase channel by a ZCCHC8 C-terminal gatekeeping domain. The architecture of a NEXT-exosome assembly points to the molecular and regulatory mechanisms with which the NEXT complex guides RNA substrates to the exosome. | |||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 4.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.4 KB 20.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.8 KB | Display | ![]() |
Images | ![]() | 97.6 KB | ||
Masks | ![]() | 64 MB | ![]() | |
Filedesc metadata | ![]() | 6.9 KB | ||
Others | ![]() ![]() ![]() | 2.3 MB 49.5 MB 49.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 664.1 KB | Display | ![]() |
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Full document | ![]() | 663.7 KB | Display | |
Data in XML | ![]() | 16.3 KB | Display | |
Data in CIF | ![]() | 21.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7z52MC ![]() 7z4yC ![]() 7z4zC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | NEXT_L_focused_on_MTR4_postprocess | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8512 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Additional map: NEXT L focused on MTR4 refine 741 denmod map
File | emd_14513_additional_1.map | ||||||||||||
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Annotation | NEXT_L_focused_on_MTR4_refine_741_denmod_map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: NEXT L focused on MTR4 half map 1
File | emd_14513_half_map_1.map | ||||||||||||
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Annotation | NEXT_L_focused_on_MTR4_half_map_1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: NEXT L focused on MTR4 half map 2
File | emd_14513_half_map_2.map | ||||||||||||
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Annotation | NEXT_L_focused_on_MTR4_half_map_2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Human NEXT dimer - focused reconstruction of the single MTR4
Entire | Name: Human NEXT dimer - focused reconstruction of the single MTR4 |
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Components |
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-Supramolecule #1: Human NEXT dimer - focused reconstruction of the single MTR4
Supramolecule | Name: Human NEXT dimer - focused reconstruction of the single MTR4 type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Exosome RNA helicase MTR4
Macromolecule | Name: Exosome RNA helicase MTR4 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA helicase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 118.32207 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GPDSMADAFG DELFSVFEGD STTAAGTKKD KEKDKGKWKG PPGSADKAGK RFDGKLQSES TNNGKNKRDV DFEGTDEPIF GKKPRIEES ITEDLSLADL MPRVKVQSVE TVEGCTHEVA LPAEEDYLPL KPRVGKAAKE YPFILDAFQR EAIQCVDNNQ S VLVSAHTS ...String: GPDSMADAFG DELFSVFEGD STTAAGTKKD KEKDKGKWKG PPGSADKAGK RFDGKLQSES TNNGKNKRDV DFEGTDEPIF GKKPRIEES ITEDLSLADL MPRVKVQSVE TVEGCTHEVA LPAEEDYLPL KPRVGKAAKE YPFILDAFQR EAIQCVDNNQ S VLVSAHTS AGKTVCAEYA IALALREKQR VIFTSPIKAL SNQKYREMYE EFQDVGLMTG DVTINPTASC LVMTTEILRS ML YRGSEVM REVAWVIFDE IHYMRDSERG VVWEETIILL PDNVHYVFLS ATIPNARQFA EWICHLHKQP CHVIYTDYRP TPL QHYIFP AGGDGLHLVV DENGDFREDN FNTAMQVLRD AGDLAKGDQK GRKGGTKGPS NVFKIVKMIM ERNFQPVIIF SFSK KDCEA YALQMTKLDF NTDEEKKMVE EVFSNAIDCL SDEDKKLPQV EHVLPLLKRG IGIHHGGLLP ILKETIEILF SEGLI KALF ATETFAMGIN MPARTVLFTN ARKFDGKDFR WISSGEYIQM SGRAGRRGMD DRGIVILMVD EKMSPTIGKQ LLKGSA DPL NSAFHLTYNM VLNLLRVEEI NPEYMLEKSF YQFQHYRAIP GVVEKVKNSE EQYNKIVIPN EESVVIYYKI RQQLAKL GK EIEEYIHKPK YCLPFLQPGR LVKVKNEGDD FGWGVVVNFS KKSNVKPNSG ELDPLYVVEV LLRCSKESLK NSATEAAK P AKPDEKGEMQ VVPVLVHLLS AISSVRLYIP KDLRPVDNRQ SVLKSIQEVQ KRFPDGIPLL DPIDDMGIQD QGLKKVIQK VEAFEHRMYS HPLHNDPNLE TVYTLCEKKA QIAIDIKSAK RELKKARTVL QMDELKCRKR VLRRLGFATS SDVIEMKGRV ACEISSADE LLLTEMMFNG LFNDLSAEQA TALLSCFVFQ ENSSEMPKLT EQLAGPLRQM QECAKRIAKV SAEAKLEIDE E TYLSSFKP HLMDVVYTWA TGATFAHICK MTDVFEGSII RCMRRLEELL RQMCQAAKAI GNTELENKFA EGITKIKRDI VF AASLYL UniProtKB: Exosome RNA helicase MTR4 |
-Macromolecule #3: Zinc finger CCHC domain-containing protein 8
Macromolecule | Name: Zinc finger CCHC domain-containing protein 8 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 78.821375 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: RSMAAEVYFG DLELFEPFDH PGESIPKPVH TRFKDDDGDE EDENGVGDAE LRERLRQCEE TIEQLRAENQ ELKRKLNILT RPSGILVND TKLDGPILQI LFMNNAISKQ YHQEIEEFVS NLVKRFEEQQ KNDVEKTSFN LLPQPSSIVL EEDHKVEESC A IKNNKEAF ...String: RSMAAEVYFG DLELFEPFDH PGESIPKPVH TRFKDDDGDE EDENGVGDAE LRERLRQCEE TIEQLRAENQ ELKRKLNILT RPSGILVND TKLDGPILQI LFMNNAISKQ YHQEIEEFVS NLVKRFEEQQ KNDVEKTSFN LLPQPSSIVL EEDHKVEESC A IKNNKEAF SVVGSVLYFT NFCLDKLGQP LLNENPQLSE GWEIPKYHQV FSHIVSLEGQ EIQVKAKRPK PHCFNCGSEE HQ MKDCPMP RNAARISEKR KEYMDACGEA NNQNFQQRYH AEEVEERFGR FKPGVISEEL QDALGVTDKS LPPFIYRMRQ LGY PPGWLK EAELENSGLA LYDGKDGTDG ETEVGEIQQN KSVTYDLSKL VNYPGFNIST PRGIPDEWRI FGSIPMQACQ QKDV FANYL TSNFQAPGVK SGNKRSSSHS SPGSPKKQKN ESNSAGSPAD MELDSDMEVP HGSQSSESFQ FQPPLPPDTP PLPRG TPPP VFTPPLPKGT PPLTPSDSPQ TRTGSGAVDE DALTLEELEE QQRRIWAALE QAESVNSDSD VPVDTPLTGN SVASSP CPN ELDLPVPEGK TSEKQTLDEP EVPEIFTKKS EAGHASSPDS EVTSLCQKEK AELAPVNTEG ALLDNGSVVP NCDISNG GS QKLFPADTSP STATKIHSPI PDMSKFATGI TPFEFENMAE STGMYLRIRS LLKNSPRNQQ KNKKASE UniProtKB: Zinc finger CCHC domain-containing protein 8 |
-Macromolecule #2: RNA (5'-R(P*UP*UP*UP*UP*U)-3')
Macromolecule | Name: RNA (5'-R(P*UP*UP*UP*UP*U)-3') / type: rna / ID: 2 / Number of copies: 1 |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 1.485872 KDa |
Sequence | String: UUUUU |
-Macromolecule #4: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Macromolecule | Name: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / type: ligand / ID: 4 / Number of copies: 1 / Formula: ANP |
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Molecular weight | Theoretical: 506.196 Da |
Chemical component information | ![]() ChemComp-ANP: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 1.705 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.3000000000000003 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |