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- EMDB-45492: Structure of the TSC:WIPI3 lysosomal recruitment complex -

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Basic information

Entry
Database: EMDB / ID: EMD-45492
TitleStructure of the TSC:WIPI3 lysosomal recruitment complex
Map dataComposite map of the tuberous sclerosis complex (TSC) and WIPI3 lysosomal docking complex.
Sample
  • Complex: TSC:WIPI3 lysosomal recruitment complex (composite map)
    • Protein or peptide: Isoform 4 of Tuberin
    • Protein or peptide: Hamartin
    • Protein or peptide: TBC1 domain family member 7
    • Protein or peptide: WD repeat domain phosphoinositide-interacting protein 3
    • Protein or peptide: Unknown fragment
KeywordsTuberous sclerosis complex / tumour suppressor / GTPase-activating proteins (GAP) / TSC-mTORC pathway / ONCOPROTEIN
Function / homology
Function and homology information


TSC1-TSC2 complex binding / memory T cell differentiation / : / TSC1-TSC2 complex / Inhibition of TSC complex formation by PKB / regulation of insulin receptor signaling pathway / cellular response to decreased oxygen levels / glycophagy / nucleophagy / negative regulation of cilium assembly ...TSC1-TSC2 complex binding / memory T cell differentiation / : / TSC1-TSC2 complex / Inhibition of TSC complex formation by PKB / regulation of insulin receptor signaling pathway / cellular response to decreased oxygen levels / glycophagy / nucleophagy / negative regulation of cilium assembly / regulation of cell-matrix adhesion / protein localization to phagophore assembly site / phagophore assembly site membrane / ATPase inhibitor activity / cardiac muscle cell differentiation / cell projection organization / Energy dependent regulation of mTOR by LKB1-AMPK / response to growth factor / negative regulation of cell size / phosphatidylinositol-3-phosphate binding / regulation of stress fiber assembly / activation of GTPase activity / negative regulation of TOR signaling / negative regulation of ATP-dependent activity / phagophore assembly site / phosphatidylinositol-3,5-bisphosphate binding / negative regulation of mitophagy / anoikis / regulation of small GTPase mediated signal transduction / protein folding chaperone complex / TBC/RABGAPs / AKT phosphorylates targets in the cytosol / extrinsic component of membrane / autophagy of mitochondrion / negative regulation of macroautophagy / positive chemotaxis / Macroautophagy / negative regulation of Wnt signaling pathway / D-glucose import / Constitutive Signaling by AKT1 E17K in Cancer / associative learning / positive regulation of macroautophagy / regulation of endocytosis / autophagosome assembly / positive regulation of focal adhesion assembly / phosphatase binding / ribosomal subunit export from nucleus / vesicle-mediated transport / negative regulation of insulin receptor signaling pathway / negative regulation of TORC1 signaling / phosphatidylinositol 3-kinase/protein kinase B signal transduction / protein folding chaperone / Hsp70 protein binding / myelination / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cellular response to starvation / GTPase activator activity / lipid droplet / insulin-like growth factor receptor signaling pathway / adult locomotory behavior / positive regulation of GTPase activity / ciliary basal body / positive regulation of protein ubiquitination / cell-matrix adhesion / neural tube closure / kidney development / TP53 Regulates Metabolic Genes / hippocampus development / response to insulin / negative regulation of protein kinase activity / Hsp90 protein binding / synapse organization / potassium ion transport / cerebral cortex development / small GTPase binding / endocytosis / protein import into nucleus / protein localization / lamellipodium / regulation of translation / heart development / protein-folding chaperone binding / cell cortex / cytoplasmic vesicle / adaptive immune response / cell population proliferation / lysosome / regulation of cell cycle / negative regulation of translation / protein stabilization / postsynaptic density / lysosomal membrane / negative regulation of cell population proliferation / perinuclear region of cytoplasm / Golgi apparatus / protein homodimerization activity / protein-containing complex / membrane / nucleus / plasma membrane
Similarity search - Function
Tuberin / Tuberin-type domain / Tuberin, N-terminal / Tuberin/Ral GTPase-activating protein subunit alpha / Tuberin / Domain of unknown function (DUF3384) / Rap/Ran-GAP domain / Rap/Ran-GAP superfamily / TBC1 domain family member 7 / TBC1 domain family member 7, domain 2 ...Tuberin / Tuberin-type domain / Tuberin, N-terminal / Tuberin/Ral GTPase-activating protein subunit alpha / Tuberin / Domain of unknown function (DUF3384) / Rap/Ran-GAP domain / Rap/Ran-GAP superfamily / TBC1 domain family member 7 / TBC1 domain family member 7, domain 2 / Rap/ran-GAP / Rap GTPase activating proteins domain profile. / Hamartin / Hamartin protein / : / PROPPIN / Rab-GTPase-TBC domain / Rab-GTPase-TBC domain superfamily / Rab-GTPase-TBC domain / TBC/rab GAP domain profile. / Armadillo-like helical / Armadillo-type fold / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Tuberin / WD repeat domain phosphoinositide-interacting protein 3 / Hamartin / TBC1 domain family member 7
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsBayly-Jones C / Lupton CJ / D'Andrea L / Ellisdon AM
Funding support United States, Australia, 3 items
OrganizationGrant numberCountry
Department of Defense (DOD, United States)W81XWH-19-1-0182 United States
Australian Research Council (ARC)DE240100992 Australia
Australian Research Council (ARC)LE170100016 Australia
CitationJournal: Sci Adv / Year: 2024
Title: Structure of the human TSC:WIPI3 lysosomal recruitment complex.
Authors: Charles Bayly-Jones / Christopher J Lupton / Laura D'Andrea / Yong-Gang Chang / Gareth D Jones / Joel R Steele / Hari Venugopal / Ralf B Schittenhelm / Michelle L Halls / Andrew M Ellisdon /
Abstract: Tuberous sclerosis complex (TSC) is targeted to the lysosomal membrane, where it hydrolyzes RAS homolog-mTORC1 binding (RHEB) from its GTP-bound to GDP-bound state, inhibiting mechanistic target of ...Tuberous sclerosis complex (TSC) is targeted to the lysosomal membrane, where it hydrolyzes RAS homolog-mTORC1 binding (RHEB) from its GTP-bound to GDP-bound state, inhibiting mechanistic target of rapamycin complex 1 (mTORC1). Loss-of-function mutations in TSC cause TSC disease, marked by excessive tumor growth. Here, we overcome a high degree of continuous conformational heterogeneity to determine the 2.8-Å cryo-electron microscopy (cryo-EM) structure of the complete human TSC in complex with the lysosomal recruitment factor WD repeat domain phosphoinositide-interacting protein 3 (WIPI3). We discover a previously undetected amino-terminal TSC1 HEAT repeat dimer that clamps onto a single TSC wing and forms a phosphatidylinositol phosphate (PIP)-binding pocket, which specifically binds monophosphorylated PIPs. These structural advances provide a model by which WIPI3 and PIP-signaling networks coordinate to recruit TSC to the lysosomal membrane to inhibit mTORC1. The high-resolution TSC structure reveals previously unrecognized mutational hotspots and uncovers crucial insights into the mechanisms of TSC dysregulation in disease.
History
DepositionJun 26, 2024-
Header (metadata) releaseDec 4, 2024-
Map releaseDec 4, 2024-
UpdateDec 4, 2024-
Current statusDec 4, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_45492.png

Downloads & links

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Map

FileDownload / File: emd_45492.map.gz / Format: CCP4 / Size: 669.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationComposite map of the tuberous sclerosis complex (TSC) and WIPI3 lysosomal docking complex.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.17 Å/pix.
x 560 pix.
= 655.2 Å		1.17 Å/pix.
x 560 pix.
= 655.2 Å		1.17 Å/pix.
x 560 pix.
= 655.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.17 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.05
Minimum - Maximum0.0 - 1.6239796
Average (Standard dev.)0.00027138324 (±0.00991092)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions560560560
Spacing560560560
CellA=B=C: 655.19995 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : TSC:WIPI3 lysosomal recruitment complex (composite map)

EntireName: TSC:WIPI3 lysosomal recruitment complex (composite map)
Components
  • Complex: TSC:WIPI3 lysosomal recruitment complex (composite map)
    • Protein or peptide: Isoform 4 of Tuberin
    • Protein or peptide: Hamartin
    • Protein or peptide: TBC1 domain family member 7
    • Protein or peptide: WD repeat domain phosphoinositide-interacting protein 3
    • Protein or peptide: Unknown fragment

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Supramolecule #1: TSC:WIPI3 lysosomal recruitment complex (composite map)

SupramoleculeName: TSC:WIPI3 lysosomal recruitment complex (composite map)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 733 KDa

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Macromolecule #1: Isoform 4 of Tuberin

MacromoleculeName: Isoform 4 of Tuberin / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 199.339 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDYKDDDDKA KPTSKDSGLK EKFKILLGLG TPRPNPRSAE GKQTEFIITA EILRELSMEC GLNNRIRMIG QICEVAKTKK FEEHAVEAL WKAVADLLQP ERPLEARHAV LALLKAIVQG QGERLGVLRA LFFKVIKDYP SNEDLHERLE VFKALTDNGR H ITYLEEEL ...String:
MDYKDDDDKA KPTSKDSGLK EKFKILLGLG TPRPNPRSAE GKQTEFIITA EILRELSMEC GLNNRIRMIG QICEVAKTKK FEEHAVEAL WKAVADLLQP ERPLEARHAV LALLKAIVQG QGERLGVLRA LFFKVIKDYP SNEDLHERLE VFKALTDNGR H ITYLEEEL ADFVLQWMDV GLSSEFLLVL VNLVKFNSCY LDEYIARMVQ MICLLCVRTA SSVDIEVSLQ VLDAVVCYNC LP AESLPLF IVTLCRTINV KELCEPCWKL MRNLLGTHLG HSAIYNMCHL MEDRAYMEDA PLLRGAVFFV GMALWGAHRL YSL RNSPTS VLPSFYQAMA CPNEVVSYEI VLSITRLIKK YRKELQVVAW DILLNIIERL LQQLQTLDSP ELRTIVHDLL TTVE ELCDQ NEFHGSQERY FELVERCADQ RPESSLLNLI SYRAQSIHPA KDGWIQNLQA LMERFFRSES RGAVRIKVLD VLSFV LLIN RQFYEEELIN SVVISQLSHI PEDKDHQVRK LATQLLVDLA EGCHTHHFNS LLDIIEKVMA RSLSPPPELE ERDVAA YSA SLEDVKTAVL GLLVILQTKL YTLPASHATR VYEMLVSHIQ LHYKHSYTLP IASSIRLQAF DFLLLLRADS LHRLGLP NK DGVVRFSPYC VCDYMEPERG SEKKTSGPLS PPTGPPGPAP AGPAVRLGSV PYSLLFRVLL QCLKQESDWK VLKLVLGR L PESLRYKVLI FTSPCSVDQL CSALCSMLSG PKTLERLRGA PEGFSRTDLH LAVVPVLTAL ISYHNYLDKT KQREMVYCL EQGLIHRCAS QCVVALSICS VEMPDIIIKA LPVLVVKLTH ISATASMAVP LLEFLSTLAR LPHLYRNFAA EQYASVFAIS LPYTNPSKF NQYIVCLAHH VIAMWFIRCR LPFRKDFVPF ITKGLRSNVL LSFDDTPEKD SFRARSTSLN ERPKSLRIAR P PKQGLNNS PPVKEFKESS AAEAFRCRSI SVSEHVVRSR IQTSLTSASL GSADENSVAQ ADDSLKNLHL ELTETCLDMM AR YVFSNFT AVPKRSPVGE FLLAGGRTKT WLVGNKLVTV TTSVGTGTRS LLGLDSGELQ SGPESSSSPG VHVRQTKEAP AKL ESQAGQ QVSRGARDRV RSMSGGHGLR VGALDVPASQ FLGSATSPGP RTAPAAKPEK ASAGTRVPVQ EKTNLAAYVP LLTQ GWAEI LVRRPTGNTS WLMSLENPLS PFSSDINNMP LQELSNALMA AERFKEHRDT ALYKSLSVPA ASTAKPPPLP RSNTD SAVV MEEGSPGEVP VLVEPPGLED VEAALGMDRR TDAYSRSSSV SSQEEKSLHA EELVGRGIPI ERVVSSEGGR PSVDLS FQP SQPLSKSSSS PELQTLQDIL GDPGDKADVG RLSPEVKARS QSGTLDGESA AWSASGEDSR GQPEGPLPSS SPRSPSG LR PRGYTISDSA PSRRGKRVER DALKSRATAS NAEKVPGINP SFVFLQLYHS PFFGDESNKP ILLPNESQSF ERSVQLLD Q IPSYDTHKIA VLYVGEGQSN SELAILSNEH GSYRYTEFLT GLGRLIELKD CQPDKVYLGG LDVCGEDGQF TYCWHDDIM QAVFHIATLM PTKDVDKHRC DKKRHLGNDF VSIVYNDSGE DFKLGTIKGQ FNFVHVIVTP LDYECNLVSL QCRKDMEGLV DTSVAKIVS DRNLPFVARQ MALHANMASQ VHHSRSNPTD IYPSKWIARL RHIKRLRQRI CEEAAYSNPS LPLVHPPSHS K APAQTPAE PTPGYEVGQR KRLISSVEDF TEFV

UniProtKB: Tuberin

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Macromolecule #2: Hamartin

MacromoleculeName: Hamartin / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 133.001609 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAQQANVGEL LAMLDSPMLG VRDDVTAVFK ENLNSDRGPM LVNTLVDYYL ETSSQPALHI LTTLQEPHDK HLLDRINEYV GKAATRLSI LSLLGHVIRL QPSWKHKLSQ APLLPSLLKC LKMDTDVVVL TTGVLVLITM LPMIPQSGKQ HLLDFFDIFG R LSSWCLKK ...String:
MAQQANVGEL LAMLDSPMLG VRDDVTAVFK ENLNSDRGPM LVNTLVDYYL ETSSQPALHI LTTLQEPHDK HLLDRINEYV GKAATRLSI LSLLGHVIRL QPSWKHKLSQ APLLPSLLKC LKMDTDVVVL TTGVLVLITM LPMIPQSGKQ HLLDFFDIFG R LSSWCLKK PGHVAEVYLV HLHASVYALF HRLYGMYPCN FVSFLRSHYS MKENLETFEE VVKPMMEHVR IHPELVTGSK DH ELDPRRW KRLETHDVVI ECAKISLDPT EASYEDGYSV SHQISARFPH RSADVTTSPY ADTQNSYGCA TSTPYSTSRL MLL NMPGQL PQTLSSPSTR LITEPPQATL WSPSMVCGMT TPPTSPGNVP PDLSHPYSKV FGTTAGGKGT PLGTPATSPP PAPL CHSDD YVHISLPQAT VTPPRKEERM DSARPCLHRQ HHLLNDRGSE EPPGSKGSVT LSDLPGFLGD LASEEDSIEK DKEEA AISR ELSEITTAEA EPVVPRGGFD SPFYRDSLPG SQRKTHSAAS SSQGASVNPE PLHSSLDKLG PDTPKQAFTP IDLPCG SAD ESPAGDRECQ TSLETSIFTP SPCKIPPPTR VGFGSGQPPP YDHLFEVALP KTAHHFVIRK TEELLKKAKG NTEEDGV PS TSPMEVLDRL IQQGADAHSK ELNKLPLPSK SVDWTHFGGS PPSDEIRTLR DQLLLLHNQL LYERFKRQQH ALRNRRLL R KVIKAAALEE HNAAMKDQLK LQEKDIQMWK VSLQKEQARY NQLQEQRDTM VTKLHSQIRQ LQHDREEFYN QSQELQTKL EDCRNMIAEL RIELKKANNK VCHTELLLSQ VSQKLSNSES VQQQMEFLNR QLLVLGEVNE LYLEQLQNKH SDTTKEVEMM KAAYRKELE KNRSHVLQQT QRLDTSQKRI LELESHLAKK DHLLLEQKKY LEDVKLQARG QLQAAESRYE AQKRITQVFE L EILDLYGR LEKDGLLKKL EEEKAEAAEA AEERLDCCND GCSDSMVGHN EEASGHNGET KTPRPSSARG SSGSRGGGGS SS SSSELST PEKPPHQRAG PFSSRWETTM GEASASIPTT VGSLPSSKSF LGMKARELFR NKSESQCDED GMTSSLSESL KTE LGKDLG VEAKIPLNLD GPHPSPPTPD SVGQLHIMDY NETHHEHSGT KLGPEQKLIS EEDLNSAVDH HHHHH

UniProtKB: Hamartin

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Macromolecule #3: TBC1 domain family member 7

MacromoleculeName: TBC1 domain family member 7 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 35.016508 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MTEDSQRNFR SVYYEKVGFR GVEEKKSLEI LLKDDRLDTE KLCTFSQRFP LPSMYRALVW KVLLGILPPH HESHAKVMMY RKEQYLDVL HALKVVRFVS DATPQAEVYL RMYQLESGKL PRSPSFPLEP DDEVFLAIAK AMEEMVEDSV DCYWITRRFV N QLNTKYRD ...String:
MTEDSQRNFR SVYYEKVGFR GVEEKKSLEI LLKDDRLDTE KLCTFSQRFP LPSMYRALVW KVLLGILPPH HESHAKVMMY RKEQYLDVL HALKVVRFVS DATPQAEVYL RMYQLESGKL PRSPSFPLEP DDEVFLAIAK AMEEMVEDSV DCYWITRRFV N QLNTKYRD SLPQLPKAFE QYLNLEDGRL LTHLRMCSAA PKLPYDLWFK RCFAGCLPES SLQRVWDKVV SGSCKILVFV AV EILLTFK IKVMALNSAE KITKFLENIP QDSSDAIVSK AIDLWHKHCG TPVHSSDYKD DDDK

UniProtKB: TBC1 domain family member 7

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Macromolecule #4: WD repeat domain phosphoinositide-interacting protein 3

MacromoleculeName: WD repeat domain phosphoinositide-interacting protein 3
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 35.222359 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MHHHHHHGLL YAGFNQDHGC FACGMENGFR VYNTDPLKEK EKQEFLEGGV GHVEMLFRCN YLALVGGGKK KVMIWDDLKK KTVIEIEFS TEVKAVKLRR DRIVVVLDSM IKVFTFTHNP HQLHVFETCY NPKGLCVLCP NSNNSLLAFP GTHTGHVQLV D LASTEKPP ...String:
MHHHHHHGLL YAGFNQDHGC FACGMENGFR VYNTDPLKEK EKQEFLEGGV GHVEMLFRCN YLALVGGGKK KVMIWDDLKK KTVIEIEFS TEVKAVKLRR DRIVVVLDSM IKVFTFTHNP HQLHVFETCY NPKGLCVLCP NSNNSLLAFP GTHTGHVQLV D LASTEKPP VDIPAHEGVL SCIALNLQGT RIATASEKGT LIRIFDTSSG HLIQELRRGS QAANIYCINF NQDASLICVS SD HGTVHIF AAEDPKSKWS FSKFQVPSGS PCICAFGTEP NAVIAICADG SYYKFLFNPK GECIRDVYAQ FLEMTDDKL

UniProtKB: WD repeat domain phosphoinositide-interacting protein 3

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Macromolecule #5: Unknown fragment

MacromoleculeName: Unknown fragment / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.039273 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)

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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

Concentration1.4 mg/mL
BufferpH: 7.6
Component:
ConcentrationFormulaName
20.0 mMHEPES4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acid
250.0 mMNaClsodium chloride
2.0 mMDTTthreo-1,4-Dimercapto-2,3-butanediol

Details: 20 mM HEPES (pH 7.6), 250 mM NaCl, 2 mM DTT
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 12807 / Average exposure time: 3.71 sec. / Average electron dose: 46.54 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.01 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1176292 / Details: Template picking, blob picking, TOPAZ, crYOLO
Startup modelType of model: OTHER / Details: Ab initio
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF
Details: The global resolution of this composite is estimated based on the voxel average of focused reconstructions.
Number images used: 200000
Initial angle assignmentType: RANDOM ASSIGNMENT / Software - Name: cryoSPARC (ver. 4.0.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software: (Name: cryoSPARC (ver. 4.0.1), RELION (ver. 4.0))
Final 3D classificationAvg.num./class: 200000 / Software - Name: RELION (ver. 4.0)

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Atomic model buiding 1

Initial model
PDB IDChain

9815

chain_id: A, source_name: AlphaFold, initial_model_type: in silico model

2574

chain_id: C, source_name: AlphaFold, initial_model_type: in silico model

5ejc

source_name: PDB, initial_model_type: experimental model

9c9i

chain_id: F, source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: OTHER / Overall B value: 96.4 / Target criteria: Cross-correlation coefficient
Output model

PDB-9ce3:
Structure of the TSC:WIPI3 lysosomal recruitment complex

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