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- EMDB-22650: Cryo-EM structure of STRIPAK complex -

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Basic information

Entry
Database: EMDB / ID: EMD-22650
TitleCryo-EM structure of STRIPAK complex
Map dataSK7 primary map
Sample
  • Complex: SK7 complex
    • Protein or peptide: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
    • Protein or peptide: Striatin-3
    • Protein or peptide: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
    • Protein or peptide: MOB-like protein phocein
    • Protein or peptide: Striatin-interacting protein 1
  • Ligand: MANGANESE (II) ION
  • Ligand: ZINC ION
  • Ligand: INOSITOL HEXAKISPHOSPHATEPhytic acid
Keywordsphosphorylation / complex / PP2A / SIGNALING PROTEIN
Function / homology
Function and homology information


FAR/SIN/STRIPAK complex / armadillo repeat domain binding / meiotic spindle elongation / Integration of energy metabolism / PP2A-mediated dephosphorylation of key metabolic factors / regulation of microtubule binding / MASTL Facilitates Mitotic Progression / mitotic sister chromatid separation / regulation of meiotic cell cycle process involved in oocyte maturation / protein phosphatase type 2A complex ...FAR/SIN/STRIPAK complex / armadillo repeat domain binding / meiotic spindle elongation / Integration of energy metabolism / PP2A-mediated dephosphorylation of key metabolic factors / regulation of microtubule binding / MASTL Facilitates Mitotic Progression / mitotic sister chromatid separation / regulation of meiotic cell cycle process involved in oocyte maturation / protein phosphatase type 2A complex / meiotic sister chromatid cohesion, centromeric / negative regulation of intracellular estrogen receptor signaling pathway / peptidyl-serine dephosphorylation / peptidyl-threonine dephosphorylation / : / positive regulation of microtubule binding / negative regulation of tyrosine phosphorylation of STAT protein / Regulation of glycolysis by fructose 2,6-bisphosphate metabolism / Inhibition of replication initiation of damaged DNA by RB1/E2F1 / female meiotic nuclear division / protein antigen binding / protein phosphatase regulator activity / ceramide metabolic process / GABA receptor binding / negative regulation of epithelial to mesenchymal transition / APC truncation mutants have impaired AXIN binding / AXIN missense mutants destabilize the destruction complex / Truncations of AMER1 destabilize the destruction complex / Initiation of Nuclear Envelope (NE) Reformation / ERKs are inactivated / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / Beta-catenin phosphorylation cascade / Signaling by GSK3beta mutants / CTNNB1 S33 mutants aren't phosphorylated / CTNNB1 S37 mutants aren't phosphorylated / CTNNB1 S45 mutants aren't phosphorylated / CTNNB1 T41 mutants aren't phosphorylated / regulation of cell morphogenesis / regulation of Wnt signaling pathway / Disassembly of the destruction complex and recruitment of AXIN to the membrane / regulation of growth / cortical actin cytoskeleton organization / negative regulation of glycolytic process through fructose-6-phosphate / Golgi cisterna membrane / positive regulation of NLRP3 inflammasome complex assembly / myosin phosphatase activity / protein serine/threonine phosphatase activity / CTLA4 inhibitory signaling / Platelet sensitization by LDL / negative regulation of MAPK cascade / protein-serine/threonine phosphatase / regulation of cell differentiation / T cell homeostasis / ERK/MAPK targets / regulation of G1/S transition of mitotic cell cycle / phosphoprotein phosphatase activity / regulation of DNA replication / mesoderm development / chromosome, centromeric region / DARPP-32 events / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / lateral plasma membrane / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / regulation of cell adhesion / Cyclin A/B1/B2 associated events during G2/M transition / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / cytoskeleton organization / Resolution of Sister Chromatid Cohesion / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / protein dephosphorylation / RNA splicing / meiotic cell cycle / protein phosphatase 2A binding / response to organic substance / protein tyrosine phosphatase activity / chromosome segregation / RHO GTPases Activate Formins / response to lead ion / regulation of protein phosphorylation / Spry regulation of FGF signaling / RAF activation / PKR-mediated signaling / Degradation of beta-catenin by the destruction complex / tau protein binding / positive regulation of protein serine/threonine kinase activity / negative regulation of cell growth / small GTPase binding / kinase binding / spindle pole / Negative regulation of MAPK pathway / Separation of Sister Chromatids / Cyclin D associated events in G1 / microtubule cytoskeleton
Similarity search - Function
Far11/STRP, N-terminal / Far11/STRP, C-terminal / Far11/STRP / N1221-like protein / Domain of unknown function (DUF3402) / N1221-like protein / Domain of unknown function (DUF3402) / Striatin, N-terminal / Striatin family / MOB kinase activator family ...Far11/STRP, N-terminal / Far11/STRP, C-terminal / Far11/STRP / N1221-like protein / Domain of unknown function (DUF3402) / N1221-like protein / Domain of unknown function (DUF3402) / Striatin, N-terminal / Striatin family / MOB kinase activator family / MOB kinase activator superfamily / Mob1/phocein family / Mob1/phocein family / : / HEAT repeat / HEAT repeat / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / HEAT repeat profile. / HEAT, type 2 / HEAT repeats / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like / Armadillo-like helical / Armadillo-type fold / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform / Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform / Striatin-3 / Striatin-interacting protein 1 / MOB-like protein phocein
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsJeong B-C / Bai XC
Funding support United States, 5 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM132275 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)CA220283 United States
Welch FoundationI-1932 United States
Welch FoundationI-1944 United States
Welch FoundationI-1702 United States
CitationJournal: Nat Struct Mol Biol / Year: 2021
Title: Cryo-EM structure of the Hippo signaling integrator human STRIPAK.
Authors: Byung-Cheon Jeong / Sung Jun Bae / Lisheng Ni / Xuewu Zhang / Xiao-Chen Bai / Xuelian Luo /
Abstract: The striatin-interacting phosphatase and kinase (STRIPAK) complex is a large, multisubunit protein phosphatase 2A (PP2A) assembly that integrates diverse cellular signals in the Hippo pathway to ...The striatin-interacting phosphatase and kinase (STRIPAK) complex is a large, multisubunit protein phosphatase 2A (PP2A) assembly that integrates diverse cellular signals in the Hippo pathway to regulate cell proliferation and survival. The architecture and assembly mechanism of this critical complex are poorly understood. Using cryo-EM, we determine the structure of the human STRIPAK core comprising PP2AA, PP2AC, STRN3, STRIP1, and MOB4 at 3.2-Å resolution. Unlike the canonical trimeric PP2A holoenzyme, STRIPAK contains four copies of STRN3 and one copy of each the PP2AA-C heterodimer, STRIP1, and MOB4. The STRN3 coiled-coil domains form an elongated homotetrameric scaffold that links the complex together. An inositol hexakisphosphate (IP) is identified as a structural cofactor of STRIP1. Mutations of key residues at subunit interfaces disrupt the integrity of STRIPAK, causing aberrant Hippo pathway activation. Thus, STRIPAK is established as a noncanonical PP2A complex with four copies of regulatory STRN3 for enhanced signal integration.
History
DepositionSep 10, 2020-
Header (metadata) releaseMar 10, 2021-
Map releaseMar 10, 2021-
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: 0.009
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  • Surface view colored by radius
  • Surface level: 0.009
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  • Surface view with fitted model
  • Atomic models: PDB-7k36
  • Surface level: 0.009
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22650.png

Downloads & links

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Map

FileDownload / File: emd_22650.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSK7 primary map
Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.01 / Movie #1: 0.009
Minimum - Maximum-0.018411795 - 0.041786376
Average (Standard dev.)0.00011531782 (±0.0013328071)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 298.8 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.830.830.83
M x/y/z360360360
origin x/y/z0.0000.0000.000
length x/y/z298.800298.800298.800
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS360360360
D min/max/mean-0.0180.0420.000

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Supplemental data

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Additional map: Focused map

Fileemd_22650_additional_1.map
AnnotationFocused map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : SK7 complex

EntireName: SK7 complex
Components
  • Complex: SK7 complex
    • Protein or peptide: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
    • Protein or peptide: Striatin-3
    • Protein or peptide: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
    • Protein or peptide: MOB-like protein phocein
    • Protein or peptide: Striatin-interacting protein 1
  • Ligand: MANGANESE (II) ION
  • Ligand: ZINC ION
  • Ligand: INOSITOL HEXAKISPHOSPHATEPhytic acid

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Supramolecule #1: SK7 complex

SupramoleculeName: SK7 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 817.8 KDa

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Macromolecule #1: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit...

MacromoleculeName: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 65.378344 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCL LPPLESLATV EETVVRDKAV ESLRAISHEH SPSDLEAHFV PLVKRLAGGD WFTSRTSACG LFSVCYPRVS S AVKAELRQ ...String:
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCL LPPLESLATV EETVVRDKAV ESLRAISHEH SPSDLEAHFV PLVKRLAGGD WFTSRTSACG LFSVCYPRVS S AVKAELRQ YFRNLCSDDT PMVRRAAASK LGEFAKVLEL DNVKSEIIPM FSNLASDEQD SVRLLAVEAC VNIAQLLPQE DL EALVMPT LRQAAEDKSW RVRYMVADKF TELQKAVGPE ITKTDLVPAF QNLMKDCEAE VRAAASHKVK EFCENLSADC REN VIMSQI LPCIKELVSD ANQHVKSALA SVIMGLSPIL GKDNTIEHLL PLFLAQLKDE CPEVRLNIIS NLDCVNEVIG IRQL SQSLL PAIVELAEDA KWRVRLAIIE YMPLLAGQLG VEFFDEKLNS LCMAWLVDHV YAIREAATSN LKKLVEKFGK EWAHA TIIP KVLAMSGDPN YLHRMTTLFC INVLSEVCGQ DITTKHMLPT VLRMAGDPVA NVRFNVAKSL QKIGPILDNS TLQSEV KPI LEKLTQDQDV DVKYFAQEAL TVLSLA

UniProtKB: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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Macromolecule #2: Striatin-3

MacromoleculeName: Striatin-3 / type: protein_or_peptide / ID: 2 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 77.833484 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MDELAGGGGG GPGMAAPPRQ QQGPGGNLGL SPGGNGAAGG GGPPASEGAG PAAGPELSRP QQYTIPGILH YIQHEWARFE MERAHWEVE RAELQARIAF LQGERKGQEN LKKDLVRRIK MLEYALKQER AKYHKLKYGT ELNQGDLKMP TFESEETKDT E APTAPQNS ...String:
MDELAGGGGG GPGMAAPPRQ QQGPGGNLGL SPGGNGAAGG GGPPASEGAG PAAGPELSRP QQYTIPGILH YIQHEWARFE MERAHWEVE RAELQARIAF LQGERKGQEN LKKDLVRRIK MLEYALKQER AKYHKLKYGT ELNQGDLKMP TFESEETKDT E APTAPQNS QLTWKQGRQL LRQYLQEVGY TDTILDVRSQ RVRSLLGLSN SEPNGSVETK NLEQILNGGE SPKQKGQEIK RS SGDVLET FNFLENADDS DEDEENDMIE GIPEGKDKHR MNKHKIGNEG LAADLTDDPD TEEALKEFDF LVTAEDGEGA GEA RSSGDG TEWAEPITFP SGGGKSFIMG SDDVLLSVLG LGDLADLTVT NDADYSYDLP ANKDAFRKTW NPKYTLRSHF DGVR ALAFH PVEPVLVTAS EDHTLKLWNL QKTVPAKKSA SLDVEPIYTF RAHIGPVLSL AISSNGEQCF SGGIDATIQW WNMPS PSVD PYDTYEPNVL AGTLVGHTDA VWGLAYSGIK NQLLSCSADG TVRLWNPQEK LPCICTYNGD KKHGIPTSVD FIGCDP AHM VTSFNTGSAV IYDLETSQSL VILSSQVDSG LQSNNHINRV VSHPTLPVTI TAHEDRHIKF FDNKTGKMIH SMVAHLD AV TSLAVDPNGI YLMSGSHDCS IRLWNLDSKT CVQEITAHRK KLDESIYDVA FHSSKAYIAS AGADALAKVF V

UniProtKB: Striatin-3

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Macromolecule #3: Serine/threonine-protein phosphatase 2A catalytic subunit alpha i...

MacromoleculeName: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: protein-serine/threonine phosphatase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 35.636152 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDR GYYSVETVTL LVALKVRYRE RITILRGNHE SRQITQVYGF YDECLRKYGN ANVWKYFTDL FDYLPLTALV D GQIFCLHG ...String:
MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDR GYYSVETVTL LVALKVRYRE RITILRGNHE SRQITQVYGF YDECLRKYGN ANVWKYFTDL FDYLPLTALV D GQIFCLHG GLSPSIDTLD HIRALDRLQE VPHEGPMCDL LWSDPDDRGG WGISPRGAGY TFGQDISETF NHANGLTLVS RA HQLVMEG YNWCHDRNVV TIFSAPNYCY RCGNQAAIME LDDTLKYSFL QFDPAPRRGE PHVTRRTPDY FL

UniProtKB: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

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Macromolecule #4: MOB-like protein phocein

MacromoleculeName: MOB-like protein phocein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.064447 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MVMAEGTAVL RRNRPGTKAQ DFYNWPDESF DEMDSTLAVQ QYIQQNIRAD CSNIDKILEP PEGQDEGVWK YEHLRQFCLE LNGLAVKLQ SECHPDTCTQ MTATEQWIFL CAAHKTPKEC PAIDYTRHTL DGAACLLNSN KYFPSRVSIK ESSVAKLGSV C RRIYRIFS ...String:
MVMAEGTAVL RRNRPGTKAQ DFYNWPDESF DEMDSTLAVQ QYIQQNIRAD CSNIDKILEP PEGQDEGVWK YEHLRQFCLE LNGLAVKLQ SECHPDTCTQ MTATEQWIFL CAAHKTPKEC PAIDYTRHTL DGAACLLNSN KYFPSRVSIK ESSVAKLGSV C RRIYRIFS HAYFHHRQIF DEYENETFLC HRFTKFVMKY NLMSKDNLIV PILEEEVQNS VSGESEA

UniProtKB: MOB-like protein phocein

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Macromolecule #5: Striatin-interacting protein 1

MacromoleculeName: Striatin-interacting protein 1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 95.695656 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MEPAVGGPGP LIVNNKQPQP PPPPPPAAAQ PPPGAPRAAA GLLPGGKARE FNRNQRKDSE GYSESPDLEF EYADTDKWAA ELSELYSYT EGPEFLMNRK CFEEDFRIHV TDKKWTELDT NQHRTHAMRL LDGLEVTARE KRLKVARAIL YVAQGTFGEC S SEAEVQSW ...String:
MEPAVGGPGP LIVNNKQPQP PPPPPPAAAQ PPPGAPRAAA GLLPGGKARE FNRNQRKDSE GYSESPDLEF EYADTDKWAA ELSELYSYT EGPEFLMNRK CFEEDFRIHV TDKKWTELDT NQHRTHAMRL LDGLEVTARE KRLKVARAIL YVAQGTFGEC S SEAEVQSW MRYNIFLLLE VGTFNALVEL LNMEIDNSAA CSSAVRKPAI SLADSTDLRV LLNIMYLIVE TVHQECEGDK AE WRTMRQT FRAELGSPLY NNEPFAIMLF GMVTKFCSGH APHFPMKKVL LLLWKTVLCT LGGFEELQSM KAEKRSILGL PPL PEDSIK VIRNMRAASP PASASDLIEQ QQKRGRREHK ALIKQDNLDA FNERDPYKAD DSREEEEEND DDNSLEGETF PLER DEVMP PPLQHPQTDR LTCPKGLPWA PKVREKDIEM FLESSRSKFI GYTLGSDTNT VVGLPRPIHE SIKTLKQHKY TSIAE VQAQ MEEEYLRSPL SGGEEEVEQV PAETLYQGLL PSLPQYMIAL LKILLAAAPT SKAKTDSINI LADVLPEEMP TTVLQS MKL GVDVNRHKEV IVKAISAVLL LLLKHFKLNH VYQFEYMAQH LVFANCIPLI LKFFNQNIMS YITAKNSISV LDYPHCV VH ELPELTAESL EAGDSNQFCW RNLFSCINLL RILNKLTKWK HSRTMMLVVF KSAPILKRAL KVKQAMMQLY VLKLLKVQ T KYLGRQWRKS NMKTMSAIYQ KVRHRLNDDW AYGNDLDARP WDFQAEECAL RANIERFNAR RYDRAHSNPD FLPVDNCLQ SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ

UniProtKB: Striatin-interacting protein 1

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Macromolecule #6: MANGANESE (II) ION

MacromoleculeName: MANGANESE (II) ION / type: ligand / ID: 6 / Number of copies: 2 / Formula: MN
Molecular weightTheoretical: 54.938 Da

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Macromolecule #7: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 7 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #8: INOSITOL HEXAKISPHOSPHATE

MacromoleculeName: INOSITOL HEXAKISPHOSPHATE / type: ligand / ID: 8 / Number of copies: 1 / Formula: IHP
Molecular weightTheoretical: 660.035 Da
Chemical component information

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE / Phytic acid

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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

Concentration2.0 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
20.0 mMHEPES4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid
100.0 mMNaClSodium chlorideSodium Chloride
1.0 mMTCEPtris(2-carboxyethyl)phosphine
2.0 mMMgCl2Magnesium Chloride
0.005 %NP-404-Nonylphenyl-polyethylene glycol
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 80 sec. / Pretreatment - Atmosphere: AIR / Details: The grid was coated with gold prior to use
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Calibrated magnification: 59524 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Detector mode: SUPER-RESOLUTION / Number real images: 4356 / Average electron dose: 64.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 2451582
Startup modelType of model: PDB ENTRY / Details: PDB ID 2NPP, 4N6J, 2YMU, 5YF4
Initial angle assignmentType: PROJECTION MATCHING
Final 3D classificationSoftware - Name: RELION (ver. 3)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 3)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3) / Number images used: 87779

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Atomic model buiding 1

Initial model
PDB IDChain

2npp

source_name: PDB, initial_model_type: experimental model

4n6j

source_name: PDB, initial_model_type: experimental model

2ymu

source_name: PDB, initial_model_type: experimental model

5yf4

source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-7k36:
Cryo-EM structure of STRIPAK complex

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