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- EMDB-14185: Human RBBP6-bound CPSF complex -

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Basic information

Entry
Database: EMDB / ID: EMD-14185
TitleHuman RBBP6-bound CPSF complex
Map data
Sample
  • Complex: Complex of RBBP6-bound CPSF
    • Protein or peptide: Cleavage and polyadenylation specificity factor subunit 1
    • Protein or peptide: Symplekin
    • Protein or peptide: Cleavage and polyadenylation specificity factor subunit 2
    • Protein or peptide: Cleavage and polyadenylation specificity factor subunit 3
    • Protein or peptide: Cleavage stimulation factor subunit 2
    • Protein or peptide: pre-mRNA 3' end processing protein WDR33
    • Protein or peptide: E3 ubiquitin-protein ligase RBBP6
    • Protein or peptide: Cleavage and polyadenylation specificity factor subunit 4
Function / homology
Function and homology information


cleavage body / co-transcriptional RNA 3'-end processing, cleavage and polyadenylation pathway / Inhibition of Host mRNA Processing and RNA Silencing / mRNA 3'-end processing by stem-loop binding and cleavage / co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway / 5'-3' RNA exonuclease activity / Processing of Intronless Pre-mRNAs / mRNA cleavage and polyadenylation specificity factor complex / somite development / nuclear stress granule ...cleavage body / co-transcriptional RNA 3'-end processing, cleavage and polyadenylation pathway / Inhibition of Host mRNA Processing and RNA Silencing / mRNA 3'-end processing by stem-loop binding and cleavage / co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway / 5'-3' RNA exonuclease activity / Processing of Intronless Pre-mRNAs / mRNA cleavage and polyadenylation specificity factor complex / somite development / nuclear stress granule / collagen trimer / mRNA 3'-UTR AU-rich region binding / mRNA 3'-end processing / Transport of Mature mRNA Derived from an Intronless Transcript / Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / mRNA 3'-end processing / tRNA processing in the nucleus / postreplication repair / RHOBTB1 GTPase cycle / RNA Polymerase II Transcription Termination / regulation of DNA replication / Processing of Capped Intron-Containing Pre-mRNA / bicellular tight junction / positive regulation of G1/S transition of mitotic cell cycle / embryonic organ development / RNA endonuclease activity / cellular response to nerve growth factor stimulus / negative regulation of protein binding / RING-type E3 ubiquitin transferase / multicellular organism growth / fibrillar center / mRNA processing / ubiquitin-protein transferase activity / sequence-specific double-stranded DNA binding / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / chromosome / ubiquitin-dependent protein catabolic process / spermatogenesis / in utero embryonic development / postsynapse / DNA replication / cytoskeleton / nuclear body / cell adhesion / protein ubiquitination / nuclear speck / ribonucleoprotein complex / intracellular membrane-bounded organelle / mRNA binding / centrosome / glutamatergic synapse / DNA damage response / nucleolus / protein kinase binding / enzyme binding / protein-containing complex / RNA binding / zinc ion binding / nucleoplasm / membrane / nucleus / metal ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Cleavage stimulation factor subunit 2, hinge domain / Zinc knuckle CX2CX3GHX4C / Zinc knuckle / Hinge domain of cleavage stimulation factor subunit 2 / DWNN domain / Transcription termination and cleavage factor, C-terminal domain / Transcription termination and cleavage factor, C-terminal domain superfamily / DWNN domain / Transcription termination and cleavage factor C-terminal / DWNN domain profile. ...Cleavage stimulation factor subunit 2, hinge domain / Zinc knuckle CX2CX3GHX4C / Zinc knuckle / Hinge domain of cleavage stimulation factor subunit 2 / DWNN domain / Transcription termination and cleavage factor, C-terminal domain / Transcription termination and cleavage factor, C-terminal domain superfamily / DWNN domain / Transcription termination and cleavage factor C-terminal / DWNN domain profile. / DWNN / Cleavage and polyadenylation specificity factor 2, C-terminal / CPSF2, metallo-hydrolase domain / Cleavage and polyadenylation factor 2 C-terminal / Cleavage and polyadenylation specificity factor subunit 2 / Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term / Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term / CPSF73-100_C / Symplekin/Pta1 / Symplekin C-terminal / Symplekin/Pta1, N-terminal / Symplekin/PTA1 N-terminal / Symplekin tight junction protein C terminal / Zinc-finger CCCH domain / Zinc-finger containing family / CPSF complex subunit CPSF4-like / Pre-mRNA 3' end processing protein Pfs2-like / Metallo-beta-lactamase superfamily domain / : / Beta-Casp domain / Beta-Casp domain / Beta-Casp domain / Zn-dependent metallo-hydrolase, RNA specificity domain / Zn-dependent metallo-hydrolase RNA specificity domain / Zinc finger C-x8-C-x5-C-x3-H type (and similar) / U-box domain / Zinc finger, CCCH-type superfamily / U-box domain / zinc finger / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / Cleavage/polyadenylation specificity factor, A subunit, N-terminal / Mono-functional DNA-alkylating methyl methanesulfonate N-term / Cleavage/polyadenylation specificity factor, A subunit, C-terminal / : / CPSF A subunit region / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase / Ring finger / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / Zinc finger RING-type profile. / RNA-binding domain superfamily / Zinc finger, RING-type / zinc finger / Zinc knuckle / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Armadillo-like helical / Armadillo-type fold / Zinc finger, RING/FYVE/PHD-type / Nucleotide-binding alpha-beta plait domain superfamily / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Cleavage and polyadenylation specificity factor subunit 4 / Cleavage stimulation factor subunit 2 / Cleavage and polyadenylation specificity factor subunit 1 / E3 ubiquitin-protein ligase RBBP6 / Symplekin / pre-mRNA 3' end processing protein WDR33 / Cleavage and polyadenylation specificity factor subunit 2 / Cleavage and polyadenylation specificity factor subunit 3
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 7.98 Å
AuthorsSandmeir F / Conti E
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Genes Dev / Year: 2022
Title: Reconstitution of 3' end processing of mammalian pre-mRNA reveals a central role of RBBP6.
Authors: Moritz Schmidt / Florian Kluge / Felix Sandmeir / Uwe Kühn / Peter Schäfer / Christian Tüting / Christian Ihling / Elena Conti / Elmar Wahle /
Abstract: The 3' ends of almost all eukaryotic mRNAs are generated in an essential two-step processing reaction: endonucleolytic cleavage of an extended precursor followed by the addition of a poly(A) tail. By ...The 3' ends of almost all eukaryotic mRNAs are generated in an essential two-step processing reaction: endonucleolytic cleavage of an extended precursor followed by the addition of a poly(A) tail. By reconstituting the reaction from overproduced and purified proteins, we provide a minimal list of 14 polypeptides that are essential and two that are stimulatory for RNA processing. In a reaction depending on the polyadenylation signal AAUAAA, the reconstituted system cleaves pre-mRNA at a single preferred site corresponding to the one used in vivo. Among the proteins, cleavage factor I stimulates cleavage but is not essential, consistent with its prominent role in alternative polyadenylation. RBBP6 is required, with structural data showing it to contact and presumably activate the endonuclease CPSF73 through its DWNN domain. The C-terminal domain of RNA polymerase II is dispensable. ATP, but not its hydrolysis, supports RNA cleavage by binding to the hClp1 subunit of cleavage factor II with submicromolar affinity.
History
DepositionJan 25, 2022-
Header (metadata) releaseMar 2, 2022-
Map releaseMar 2, 2022-
UpdateMar 2, 2022-
Current statusMar 2, 2022Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.31
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.31
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_14185.png

Downloads & links

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Map

FileDownload / File: emd_14185.map.gz / Format: CCP4 / Size: 274.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 416 pix.
= 455.104 Å		1.09 Å/pix.
x 416 pix.
= 455.104 Å		1.09 Å/pix.
x 416 pix.
= 455.104 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.094 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.31 / Movie #1: 0.31
Minimum - Maximum-1.1611375 - 2.0819485
Average (Standard dev.)0.0023898948 (±0.064156316)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions416416416
Spacing416416416
CellA=B=C: 455.104 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0941.0941.094
M x/y/z416416416
origin x/y/z0.0000.0000.000
length x/y/z455.104455.104455.104
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ450450450
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS416416416
D min/max/mean-1.1612.0820.002

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Supplemental data

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Sample components

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Entire : Complex of RBBP6-bound CPSF

EntireName: Complex of RBBP6-bound CPSF
Components
  • Complex: Complex of RBBP6-bound CPSF
    • Protein or peptide: Cleavage and polyadenylation specificity factor subunit 1
    • Protein or peptide: Symplekin
    • Protein or peptide: Cleavage and polyadenylation specificity factor subunit 2
    • Protein or peptide: Cleavage and polyadenylation specificity factor subunit 3
    • Protein or peptide: Cleavage stimulation factor subunit 2
    • Protein or peptide: pre-mRNA 3' end processing protein WDR33
    • Protein or peptide: E3 ubiquitin-protein ligase RBBP6
    • Protein or peptide: Cleavage and polyadenylation specificity factor subunit 4

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Supramolecule #1: Complex of RBBP6-bound CPSF

SupramoleculeName: Complex of RBBP6-bound CPSF / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)

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Macromolecule #1: Cleavage and polyadenylation specificity factor subunit 1

MacromoleculeName: Cleavage and polyadenylation specificity factor subunit 1
type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MYAVYKQAHP PTGLEFSMYC NFFNNSERNL VVAGTSQLYV YRLNRDAEAL TKNDRSTEGK AHREKLELAA SFSFFGNVMS MASVQLAGAK RDALLLSFKD AKLSVVEYDP GTHDLKTLSL HYFEEPELRD GFVQNVHTPR VRVDPDGRCA AMLVYGTRLV VLPFRRESLA ...String:
MYAVYKQAHP PTGLEFSMYC NFFNNSERNL VVAGTSQLYV YRLNRDAEAL TKNDRSTEGK AHREKLELAA SFSFFGNVMS MASVQLAGAK RDALLLSFKD AKLSVVEYDP GTHDLKTLSL HYFEEPELRD GFVQNVHTPR VRVDPDGRCA AMLVYGTRLV VLPFRRESLA EEHEGLVGEG QRSSFLPSYI IDVRALDEKL LNIIDLQFLH GYYEPTLLIL FEPNQTWPGR VAVRQDTCSI VAISLNITQK VHPVIWSLTS LPFDCTQALA VPKPIGGVVV FAVNSLLYLN QSVPPYGVAL NSLTTGTTAF PLRTQEGVRI TLDCAQATFI SYDKMVISLK GGEIYVLTLI TDGMRSVRAF HFDKAAASVL TTSMVTMEPG YLFLGSRLGN SLLLKYTEKL QEPPASAVRE AADKEEPPSK KKRVDATAGW SAAGKSVPQD EVDEIEVYGS EAQSGTQLAT YSFEVCDSIL NIGPCANAAV GEPAFLSEEF QNSPEPDLEI VVCSGHGKNG ALSVLQKSIR PQVVTTFELP GCYDMWTVIA PVRKEEEDNP KGEGTEQEPS TTPEADDDGR RHGFLILSRE DSTMILQTGQ EIMELDTSGF ATQGPTVFAG NIGDNRYIVQ VSPLGIRLLE GVNQLHFIPV DLGAPIVQCA VADPYVVIMS AEGHVTMFLL KSDSYGGRHH RLALHKPPLH HQSKVITLCL YRDLSGMFTT ESRLGGARDE LGGRSGPEAE GLGSETSPTV DDEEEMLYGD SGSLFSPSKE EARRSSQPPA DRDPAPFRAE PTHWCLLVRE NGTMEIYQLP DWRLVFLVKN FPVGQRVLVD SSFGQPTTQG EARREEATRQ GELPLVKEVL LVALGSRQSR PYLLVHVDQE LLIYEAFPHD SQLGQGNLKV RFKKVPHNIN FREKKPKPSK KKAEGGGAEE GAGARGRVAR FRYFEDIYGY SGVFICGPSP HWLLVTGRGA LRLHPMAIDG PVDSFAPFHN VNCPRGFLYF NRQGELRISV LPAYLSYDAP WPVRKIPLRC TAHYVAYHVE SKVYAVATST NTPCARIPRM TGEEKEFETI ERDERYIHPQ QEAFSIQLIS PVSWEAIPNA RIELQEWEHV TCMKTVSLRS EETVSGLKGY VAAGTCLMQG EEVTCRGRIL IMDVIEVVPE PGQPLTKNKF KVLYEKEQKG PVTALCHCNG HLVSAIGQKI FLWSLRASEL TGMAFIDTQL YIHQMISVKN FILAADVMKS ISLLRYQEES KTLSLVSRDA KPLEVYSVDF MVDNAQLGFL VSDRDRNLMV YMYLPEAKES FGGMRLLRRA DFHVGAHVNT FWRTPCRGAT EGLSKKSVVW ENKHITWFAT LDGGIGLLLP MQEKTYRRLL MLQNALTTML PHHAGLNPRA FRMLHVDRRT LQNAVRNVLD GELLNRYLYL STMERSELAK KIGTTPDIIL DDLLETDRVT AHF

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Macromolecule #2: Symplekin

MacromoleculeName: Symplekin / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KTAGLEVLFQ GPMASGSGDS VTRRSVASQF FTQEEGPGID GMTTSERVVD LLNQAALITN DSKITVLKQV QELIINKDPT LLDNFLDEII AFQADKSIEV RKFVIGFIEE ACKRDIELLL KLIANLNMLL RDENVNVVKK ...String:
MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KTAGLEVLFQ GPMASGSGDS VTRRSVASQF FTQEEGPGID GMTTSERVVD LLNQAALITN DSKITVLKQV QELIINKDPT LLDNFLDEII AFQADKSIEV RKFVIGFIEE ACKRDIELLL KLIANLNMLL RDENVNVVKK AILTMTQLYK VALQWMVKSR VISELQEACW DMVSAMAGDI ILLLDSDNDG IRTHAIKFVE GLIVTLSPRM ADSEIPRRQE HDISLDRIPR DHPYIQYNVL WEEGKAALEQ LLKFMVHPAI SSINLTTALG SLANIARQRP MFMSEVIQAY ETLHANLPPT LAKSQVSSVR KNLKLHLLSV LKHPASLEFQ AQITTLLVDL GTPQAEIARN MPSSKDTRKR PRDDSDSTLK KMKLEPNLGE DDEDKDLEPG PSGTSKASAQ ISGQSDTDIT AEFLQPLLTP DNVANLVLIS MVYLPEAMPA SFQAIYTPVE SAGTEAQIKH LARLMATQMT AAGLGPGVEQ TKQCKEEPKE EKVVKTESVL IKRRLSAQGQ AISVVGSLSS MSPLEEEAPQ AKRRPEPIIP VTQPRLAGAG GRKKIFRLSD VLKPLTDAQV EAMKLGAVKR ILRAEKAVAC SGAAQVRIKI LASLVTQFNS GLKAEVLSFI LEDVRARLDL AFAWLYQEYN AYLAAGASGS LDKYEDCLIR LLSGLQEKPD QKDGIFTKVV LEAPLITESA LEVVRKYCED ESRTYLGMST LRDLIFKRPS RQFQYLHVLL DLSSHEKDKV RSQALLFIKR MYEKEQLREY VEKFALNYLQ LLVHPNPPSV LFGADKDTEV AAPWTEETVK QCLYLYLALL PQNHKLIHEL AAVYTEAIAD IKRTVLRVIE QPIRGMGMNS PELLLLVENC PKGAETLVTR CLHSLTDKVP PSPELVKRVR DLYHKRLPDV RFLIPVLNGL EKKEVIQALP KLIKLNPIVV KEVFNRLLGT QHGEGNSALS PLNPGELLIA LHNIDSVKCD MKSIIKATNL CFAERNVYTS EVLAVVMQQL MEQSPLPMLL MRTVIQSLTM YPRLGGFVMN ILSRLIMKQV WKYPKVWEGF IKCCQRTKPQ SFQVILQLPP QQLGAVFDKC PELREPLLAH VRSFTPHQQA HIPNSIMTIL EASGKQEPEA KEAPAGPLEE DDLEPLTLAP APAPRPPQDL IGLRLAQEKA LKRQLEEEQK LKPGGVGAPS SSSPSPSPSA RPGPPPSEEA MDFREEGPEC ETPGIFISMD DDSGLTEAAL LDSSLEGPLP KETAAGGLTL KEERSPQTLA PVGEDAMKTP SPAAEDAREP EAKGNS

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Macromolecule #3: Cleavage and polyadenylation specificity factor subunit 2

MacromoleculeName: Cleavage and polyadenylation specificity factor subunit 2
type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SMDIIDSLRK HVHQIDAVLL SHPDPLHLGA LPYAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI ...String:
MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SMDIIDSLRK HVHQIDAVLL SHPDPLHLGA LPYAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR EIHLNGCSLE MLSRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK NSIILTYRTT PGTLARFLID NPSEKVTEIE LRKRVKLEGK ELEEYLEKEK LKKEAAKKLE QSKEADIDSS DESDIEEDID QPSAHKTKHD LMMKGEGSRK GSFFKQAKKS YPMFPAPEER IKWDEYGEII KPEDFLVPEL QATEEEKSKL ESGLTNGDEP MDQDLSDVPT KCISTTESIE IKARVTYIDY EGRSDGDSIK KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE GELKDDGEDS EMQVEAPSDS SVIAQQKAMK SLFGDDEKET GEESEIIPTL EPLPPHEVPG HQSVFMNEPR LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV RRTETGRIGL EGCLCQDFYR IRDLLYEQYA IV

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Macromolecule #4: Cleavage and polyadenylation specificity factor subunit 3

MacromoleculeName: Cleavage and polyadenylation specificity factor subunit 3
type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MSAIPAEESD QLLIRPLGAG QEVGRSCIIL EFKGRKIMLD CGIHPGLEGM DALPYIDLID PAEIDLLLIS HFHLDHCGAL PWFLQKTSFK GRTFMTHATK AIYRWLLSDY VKVSNISADD MLYTETDLEE SMDKIETINF HEVKEVAGIK FWCYHAGHVL GAAMFMIEIA ...String:
MSAIPAEESD QLLIRPLGAG QEVGRSCIIL EFKGRKIMLD CGIHPGLEGM DALPYIDLID PAEIDLLLIS HFHLDHCGAL PWFLQKTSFK GRTFMTHATK AIYRWLLSDY VKVSNISADD MLYTETDLEE SMDKIETINF HEVKEVAGIK FWCYHAGHVL GAAMFMIEIA GVKLLYTGDF SRQEDRHLMA AEIPNIKPDI LIIESTYGTH IHEKREEREA RFCNTVHDIV NRGGRGLIPV FALGRAQELL LILDEYWQNH PELHDIPIYY ASSLAKKCMA VYQTYVNAMN DKIRKQININ NPFVFKHISN LKSMDHFDDI GPSVVMASPG MMQSGLSREL FESWCTDKRN GVIIAGYCVE GTLAKHIMSE PEEITTMSGQ KLPLKMSVDY ISFSAHTDYQ QTSEFIRALK PPHVILVHGE QNEMARLKAA LIREYEDNDE VHIEVHNPRN TEAVTLNFRG EKLAKVMGFL ADKKPEQGQR VSGILVKRNF NYHILSPCDL SNYTDLAMST VKQTQAIPYT GPFNLLCYQL QKLTGDVEEL EIQEKPALKV FKNITVIQEP GMVVLEWLAN PSNDMYADTV TTVILEVQSN PKIRKGAVQK VSKKLEMHVY SKRLEIMLQD IFGEDCVSVK DDSILSVTVD GKTANLNLET RTVECEEGSE DDESLREMVE LAAQRLYEAL TPVH

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Macromolecule #5: Cleavage stimulation factor subunit 2

MacromoleculeName: Cleavage stimulation factor subunit 2 / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGETIS PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ...String:
MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGETIS PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR IVDPEIALKI LHRQTNIPTL IAGNPQPVHG AGPGSGSNVS MNQQNPQAPQ AQSLGGMHVN GAPPLMQASM QGGVPAPGQM PAAVTGPGPG SLAPGGGMQA QVGMPGSGPV SMERGQVPMQ DPRAAMQRGS LPANVPTPRG LLGDAPNDPR GGTLLSVTGE VEPRGYLGPP HQGPPMHHVP GHESRGPPPH ELRGGPLPEP RPLMAEPRGP MLDQRGPPLD GRGGRDPRGI DARGMEARAM EARGLDARGL EARAMEARAM EARAMEARAM EARAMEVRGM EARGMDTRGP VPGPRGPIPS GMQGPSPINM GAVVPQGSRQ VPVMQGTGMQ GASIQGGSQP GGFSPGQNQV TPQDHEKAAL IMQVLQLTAD QIAMLPPEQR QSILILKEQI QKSTGAP

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Macromolecule #6: pre-mRNA 3' end processing protein WDR33

MacromoleculeName: pre-mRNA 3' end processing protein WDR33 / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MATEIGSPPR FFHMPRFQHQ APRQLFYKRP DFAQQQAMQQ LTFDGKRMRK AVNRKTIDYN PSVIKYLENR IWQRDQRDMR AIQPDAGYYN DLVPPIGMLN NPMNAVTTKF VRTSTNKVKC PVFVVRWTPE GRRLVTGASS GEFTLWNGLT FNFETILQAH DSPVRAMTWS ...String:
MATEIGSPPR FFHMPRFQHQ APRQLFYKRP DFAQQQAMQQ LTFDGKRMRK AVNRKTIDYN PSVIKYLENR IWQRDQRDMR AIQPDAGYYN DLVPPIGMLN NPMNAVTTKF VRTSTNKVKC PVFVVRWTPE GRRLVTGASS GEFTLWNGLT FNFETILQAH DSPVRAMTWS HNDMWMLTAD HGGYVKYWQS NMNNVKMFQA HKEAIREASF SPTDNKFATC SDDGTVRIWD FLRCHEERIL RGHGADVKCV DWHPTKGLVV SGSKDSQQPI KFWDPKTGQS LATLHAHKNT VMEVKLNLNG NWLLTASRDH LCKLFDIRNL KEELQVFRGH KKEATAVAWH PVHEGLFASG GSDGSLLFWH VGVEKEVGGM EMAHEGMIWS LAWHPLGHIL CSGSNDHTSK FWTRNRPGDK MRD

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Macromolecule #7: E3 ubiquitin-protein ligase RBBP6

MacromoleculeName: E3 ubiquitin-protein ligase RBBP6 / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: GPMSCVHYKF SSKLNYDTVT FDGLHISLCD LKKQIMGREK LKAADCDLQI TNAQTKEEYT DDNALIPKNS SVIVRRIPIG GVKSTSKTYV ISRTEPAMAT TKAIDDSSAS ISLAQLTKTA NLAEANASEE DKIKAMMSQS GHEYDPINYM KKPLGPPPPS YTCFRCGKPG ...String:
GPMSCVHYKF SSKLNYDTVT FDGLHISLCD LKKQIMGREK LKAADCDLQI TNAQTKEEYT DDNALIPKNS SVIVRRIPIG GVKSTSKTYV ISRTEPAMAT TKAIDDSSAS ISLAQLTKTA NLAEANASEE DKIKAMMSQS GHEYDPINYM KKPLGPPPPS YTCFRCGKPG HYIKNCPTNG DKNFESGPRI KKSTGIPRSF MMEVKDPNMK GAMLTNTGKY AIPTIDAEAY AIGKKEKPPF LPEEPSSSSE EDDPIPDELL CLICKDIMTD AVVIPCCGNS YCDECIRTAL LESDEHTCPT CHQNDVSPDA LIANKFLRQA VNNFKNETGY TKRLRKQ

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Macromolecule #8: Cleavage and polyadenylation specificity factor subunit 4

MacromoleculeName: Cleavage and polyadenylation specificity factor subunit 4
type: protein_or_peptide / ID: 8 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MQEIIASVDH IKFDLEIAVE QQLGAQPLPF PGMDKSGAAV CEFFLKAACG KGGMCPFRHI SGEKTVVCKH WLRGLCKKGD QCEFLHEYDM TKMPECYFYS KFGECSNKEC PFLHIDPESK IKDCPWYDRG FCKHGPLCRH RHTRRVICVN YLVGFCPEGP SCKFMHPRFE ...String:
MQEIIASVDH IKFDLEIAVE QQLGAQPLPF PGMDKSGAAV CEFFLKAACG KGGMCPFRHI SGEKTVVCKH WLRGLCKKGD QCEFLHEYDM TKMPECYFYS KFGECSNKEC PFLHIDPESK IKDCPWYDRG FCKHGPLCRH RHTRRVICVN YLVGFCPEGP SCKFMHPRFE LPMGTTEQPP LPQQTQPPAK QRTPQVIGVM QSQNSSAGNR GPRPLEQVTC YKCGEKGHYA NRCTKGHLAF LSGQ

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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: 7.9
GridModel: Quantifoil R1.2/1.3
VitrificationCryogen name: ETHANE-PROPANE / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 7462 / Average exposure time: 9.5 sec. / Average electron dose: 63.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.7000000000000001 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionResolution.type: BY AUTHOR / Resolution: 7.98 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 69204
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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