[English] 日本語
Yorodumi
- EMDB-43197: Cryo-EM structure of FoxA1 and GATA4 in complex with ALBN1 nucleosome -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-43197
TitleCryo-EM structure of FoxA1 and GATA4 in complex with ALBN1 nucleosome
Map datamain map
Sample
  • Complex: FoxA1 and GATA4 in complx with 186bp ALBN1 nucleosome
    • Protein or peptide: Histone H3.1
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-B/E
    • Protein or peptide: Histone H2B type 1-J
    • DNA: DNA (171-MER)
    • DNA: DNA (171-MER)
    • Protein or peptide: Hepatocyte nuclear factor 3-alpha
    • Protein or peptide: Maltose/maltodextrin-binding periplasmic protein,Transcription factor GATA-4
  • Ligand: ZINC ION
Keywordsnucleosome / pioneer transcription factors / DNA binding proteins / transcription / chromatin / NUCLEAR PROTEIN / NUCLEAR PROTEIN-DNA complex
Function / homology
Function and homology information


alveolar secondary septum development / respiratory basal cell differentiation / positive regulation of dopaminergic neuron differentiation / atrial septum secundum morphogenesis / atrioventricular valve formation / embryonic heart tube anterior/posterior pattern specification / transdifferentiation / mesenchymal-epithelial cell signaling involved in prostate gland development / Formation of lateral plate mesoderm / anatomical structure formation involved in morphogenesis ...alveolar secondary septum development / respiratory basal cell differentiation / positive regulation of dopaminergic neuron differentiation / atrial septum secundum morphogenesis / atrioventricular valve formation / embryonic heart tube anterior/posterior pattern specification / transdifferentiation / mesenchymal-epithelial cell signaling involved in prostate gland development / Formation of lateral plate mesoderm / anatomical structure formation involved in morphogenesis / cardiac right ventricle morphogenesis / intestinal epithelial cell differentiation / prostate gland stromal morphogenesis / positive regulation of cell-cell adhesion mediated by cadherin / atrioventricular node development / co-SMAD binding / epithelial cell maturation involved in prostate gland development / atrial septum morphogenesis / cardiac muscle tissue regeneration / cell growth involved in cardiac muscle cell development / Transcriptional regulation of testis differentiation / cardiac ventricle morphogenesis / neuron fate specification / endocardial cushion development / Physiological factors / atrial septum primum morphogenesis / atrioventricular canal development / lung epithelial cell differentiation / embryonic foregut morphogenesis / secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development / YAP1- and WWTR1 (TAZ)-stimulated gene expression / Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) / dorsal/ventral neural tube patterning / Formation of definitive endoderm / prostate gland epithelium morphogenesis / endoderm development / dopaminergic neuron differentiation / Formation of axial mesoderm / positive regulation of BMP signaling pathway / Developmental Lineage of Pancreatic Acinar Cells / positive regulation of smoothened signaling pathway / hormone metabolic process / response to vitamin A / aortic valve morphogenesis / regulation of cardiac muscle cell contraction / Cardiogenesis / negative regulation of cardiac muscle cell apoptotic process / ventricular septum development / negative regulation of epithelial to mesenchymal transition / smoothened signaling pathway / positive regulation of intracellular estrogen receptor signaling pathway / DNA-binding transcription activator activity / NFAT protein binding / epithelial tube branching involved in lung morphogenesis / detection of maltose stimulus / heart looping / maltose transport complex / microvillus / carbohydrate transport / positive regulation of vascular endothelial growth factor production / negative regulation of apoptotic signaling pathway / carbohydrate transmembrane transporter activity / anatomical structure morphogenesis / cell fate commitment / maltose binding / negative regulation of tumor necrosis factor-mediated signaling pathway / maltose transport / maltodextrin transmembrane transport / response to mechanical stimulus / positive regulation of DNA-binding transcription factor activity / negative regulation of megakaryocyte differentiation / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / CENP-A containing nucleosome / Packaging Of Telomere Ends / Notch signaling pathway / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / telomere organization / Interleukin-7 signaling / Inhibition of DNA recombination at telomere / negative regulation of autophagy / RNA Polymerase I Promoter Opening / Meiotic synapsis / positive regulation of mitotic cell cycle / ATP-binding cassette (ABC) transporter complex / Assembly of the ORC complex at the origin of replication / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / epigenetic regulation of gene expression / Chromatin modifications during the maternal to zygotic transition (MZT) / SIRT1 negatively regulates rRNA expression
Similarity search - Function
GATA-type transcription activator, N-terminal / Transcription factor GATA-4/5/6 / GATA-type transcription activator, N-terminal / Forkhead box protein, C-terminal / HNF3 C-terminal domain / Fork-head N-terminal / Forkhead N-terminal region / : / Transcription factor GATA / Fork head domain conserved site1 ...GATA-type transcription activator, N-terminal / Transcription factor GATA-4/5/6 / GATA-type transcription activator, N-terminal / Forkhead box protein, C-terminal / HNF3 C-terminal domain / Fork-head N-terminal / Forkhead N-terminal region / : / Transcription factor GATA / Fork head domain conserved site1 / Fork head domain signature 1. / GATA-type zinc finger domain. / GATA-type zinc finger domain profile. / zinc finger binding to DNA consensus sequence [AT]GATA[AG] / GATA zinc finger / Zinc finger, GATA-type / Fork head domain / Forkhead domain / Fork head domain profile. / FORKHEAD / Fork head domain conserved site 2 / Fork head domain signature 2. / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / : / Histone H2B signature. / Histone H2A conserved site / Histone H2A signature. / Histone H2B / Histone H2B / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone 2A / Histone H2A / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Zinc finger, NHR/GATA-type / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
Histone H2A type 1-B/E / Histone H2B type 1-J / Maltose/maltodextrin-binding periplasmic protein / Transcription factor GATA-4 / Hepatocyte nuclear factor 3-alpha / Histone H4 / Histone H3.1
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.48 Å
AuthorsZhou BR / Bai Y
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)Intramural Research Program United States
CitationJournal: Mol Cell / Year: 2024
Title: Structural insights into the cooperative nucleosome recognition and chromatin opening by FOXA1 and GATA4.
Authors: Bing-Rui Zhou / Hanqiao Feng / Furong Huang / Iris Zhu / Stephanie Portillo-Ledesma / Dan Shi / Kenneth S Zaret / Tamar Schlick / David Landsman / Qianben Wang / Yawen Bai /
Abstract: Mouse FOXA1 and GATA4 are prototypes of pioneer factors, initiating liver cell development by binding to the N1 nucleosome in the enhancer of the ALB1 gene. Using cryoelectron microscopy (cryo-EM), ...Mouse FOXA1 and GATA4 are prototypes of pioneer factors, initiating liver cell development by binding to the N1 nucleosome in the enhancer of the ALB1 gene. Using cryoelectron microscopy (cryo-EM), we determined the structures of the free N1 nucleosome and its complexes with FOXA1 and GATA4, both individually and in combination. We found that the DNA-binding domains of FOXA1 and GATA4 mainly recognize the linker DNA and an internal site in the nucleosome, respectively, whereas their intrinsically disordered regions interact with the acidic patch on histone H2A-H2B. FOXA1 efficiently enhances GATA4 binding by repositioning the N1 nucleosome. In vivo DNA editing and bioinformatics analyses suggest that the co-binding mode of FOXA1 and GATA4 plays important roles in regulating genes involved in liver cell functions. Our results reveal the mechanism whereby FOXA1 and GATA4 cooperatively bind to the nucleosome through nucleosome repositioning, opening chromatin by bending linker DNA and obstructing nucleosome packing.
History
DepositionDec 22, 2023-
Header (metadata) releaseAug 7, 2024-
Map releaseAug 7, 2024-
UpdateMay 28, 2025-
Current statusMay 28, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

emd_43197.png

Downloads & links

-
Map

FileDownload / File: emd_43197.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmain map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 300 pix.
= 316.8 Å		1.06 Å/pix.
x 300 pix.
= 316.8 Å		1.06 Å/pix.
x 300 pix.
= 316.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.056 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.004
Minimum - Maximum-0.021857578 - 0.062828355
Average (Standard dev.)0.000058804613 (±0.0011835682)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 316.8 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: half B

Fileemd_43197_half_map_1.map
Annotationhalf B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: half A

Fileemd_43197_half_map_2.map
Annotationhalf A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

+
Entire : FoxA1 and GATA4 in complx with 186bp ALBN1 nucleosome

EntireName: FoxA1 and GATA4 in complx with 186bp ALBN1 nucleosome
Components
  • Complex: FoxA1 and GATA4 in complx with 186bp ALBN1 nucleosome
    • Protein or peptide: Histone H3.1
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-B/E
    • Protein or peptide: Histone H2B type 1-J
    • DNA: DNA (171-MER)
    • DNA: DNA (171-MER)
    • Protein or peptide: Hepatocyte nuclear factor 3-alpha
    • Protein or peptide: Maltose/maltodextrin-binding periplasmic protein,Transcription factor GATA-4
  • Ligand: ZINC ION

+
Supramolecule #1: FoxA1 and GATA4 in complx with 186bp ALBN1 nucleosome

SupramoleculeName: FoxA1 and GATA4 in complx with 186bp ALBN1 nucleosome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human)

+
Macromolecule #1: Histone H3.1

MacromoleculeName: Histone H3.1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.437167 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEACEA YLVGLFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.1

+
Macromolecule #2: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.394426 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG

UniProtKB: Histone H4

+
Macromolecule #3: Histone H2A type 1-B/E

MacromoleculeName: Histone H2A type 1-B/E / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.165551 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIR NDEELNKLLG RVTIAQGGVL PNIQAVLLPK KTESHHKAKG K

UniProtKB: Histone H2A type 1-B/E

+
Macromolecule #4: Histone H2B type 1-J

MacromoleculeName: Histone H2B type 1-J / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.935239 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSAK

UniProtKB: Histone H2B type 1-J

+
Macromolecule #7: Hepatocyte nuclear factor 3-alpha

MacromoleculeName: Hepatocyte nuclear factor 3-alpha / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 50.022562 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MLGTVKMEGH ETSDWNSYYA DTQEAYSSVP VSNMNSGLGS MNSMNTYMTM NTMTTSGNMT PASFNMSYAN PGLGAGLSPG AVAGMPGGS AGAMNSMTAA GVTAMGTALS PSGMGAMGAQ QAASMNGLGP YAAAMNPCMS PMAYAPSNLG RSRAGGGGDA K TFKRSYPH ...String:
MLGTVKMEGH ETSDWNSYYA DTQEAYSSVP VSNMNSGLGS MNSMNTYMTM NTMTTSGNMT PASFNMSYAN PGLGAGLSPG AVAGMPGGS AGAMNSMTAA GVTAMGTALS PSGMGAMGAQ QAASMNGLGP YAAAMNPCMS PMAYAPSNLG RSRAGGGGDA K TFKRSYPH AKPPYSYISL ITMAIQQAPS KMLTLSEIYQ WIMDLFPYYR QNQQRWQNSI RHSLSFNDCF VKVARSPDKP GK GSYWTLH PDSGNMFENG CYLRRQKRFK CEKQPGAGGG GGSGSGGSGA KGGPESRKDP SGASNPSADS PLHRGVHGKT GQL EGAPAP GPAASPQTLD HSGATATGGA SELKTPASST APPISSGPGA LASVPASHPA HGLAPHESQL HLKGDPHYSF NHPF SINNL MSSSEQQHKL DFKAYEQALQ YSPYGSTLPA SLPLGSASVT TRSPIEPSAL EPAYYQGVYS RPVLNTSHHH HHH

UniProtKB: Hepatocyte nuclear factor 3-alpha

+
Macromolecule #8: Maltose/maltodextrin-binding periplasmic protein,Transcription fa...

MacromoleculeName: Maltose/maltodextrin-binding periplasmic protein,Transcription factor GATA-4
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 87.880258 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MGSSHHHHHH GSSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGL LAEITPDKAF QDKLYPFTWD AVRYNGKLIA YPIAVEALSL IYNKDLLPNP PKTWEEIPAL DKELKAKGKS A LMFNLQEP ...String:
MGSSHHHHHH GSSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGL LAEITPDKAF QDKLYPFTWD AVRYNGKLIA YPIAVEALSL IYNKDLLPNP PKTWEEIPAL DKELKAKGKS A LMFNLQEP YFTWPLIAAD GGYAFKYENG KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE AAFNKGETAM TI NGPWAWS NIDTSKVNYG VTVLPTFKGQ PSKPFVGVLS AGINAASPNK ELAKEFLENY LLTDEGLEAV NKDKPLGAVA LKS YEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTNGIEEN LYFQSNAMYQ SLAM AANHG PPPGAYEAGG PGAFMHGAGA ASSPVYVPTP RVPSSVLGLS YLQGGGAGSA SGGASGGSSG GAASGAGPGT QQGSP GWSQ AGADGAAYTP PPVSPRFSFP GTTGSLAAAA AAAAAREAAA YSSGGGAAGA GLAGREQYGR AGFAGSYSSP YPAYMA DVG ASWAAAAAAS AGPFDSPVLH SLPGRANPAA RHPNLDMFDD FSEGRECVNC GAMSTPLWRR DGTGHYLCNA CGLYHKM NG INRPLIKPQR RLSASRRVGL SCANCQTTTT TLWRRNAEGE PVCNACGLYM KLHGVPRPLA MRKEGIQTRK RKPKNLNK S KTPAAPSGSE SLPPASGASS NSSNATTSSS EEMRPIKTEP GLSSHYGHSS SVSQTFSVSA MSGHGPSIHP VLSALKLSP QGYASPVSQS PQTSSKQDSW NSLVLADSHG DIITA

UniProtKB: Maltose/maltodextrin-binding periplasmic protein, Transcription factor GATA-4

+
Macromolecule #5: DNA (171-MER)

MacromoleculeName: DNA (171-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 57.399637 KDa
SequenceString: (DA)(DT)(DC)(DC)(DG)(DA)(DG)(DA)(DT)(DG) (DG)(DT)(DA)(DC)(DT)(DT)(DT)(DG)(DT)(DG) (DT)(DC)(DT)(DC)(DC)(DT)(DG)(DC)(DT) (DC)(DT)(DG)(DT)(DC)(DA)(DG)(DC)(DA)(DG) (DG) (DG)(DC)(DA)(DC)(DT)(DG) ...String:
(DA)(DT)(DC)(DC)(DG)(DA)(DG)(DA)(DT)(DG) (DG)(DT)(DA)(DC)(DT)(DT)(DT)(DG)(DT)(DG) (DT)(DC)(DT)(DC)(DC)(DT)(DG)(DC)(DT) (DC)(DT)(DG)(DT)(DC)(DA)(DG)(DC)(DA)(DG) (DG) (DG)(DC)(DA)(DC)(DT)(DG)(DT)(DA) (DC)(DT)(DT)(DG)(DC)(DT)(DG)(DA)(DT)(DA) (DC)(DC) (DA)(DG)(DG)(DG)(DA)(DA)(DT) (DG)(DT)(DT)(DT)(DG)(DT)(DT)(DC)(DT)(DT) (DA)(DA)(DA) (DT)(DA)(DC)(DC)(DA)(DT) (DC)(DA)(DT)(DT)(DC)(DC)(DG)(DG)(DA)(DC) (DG)(DT)(DG)(DT) (DT)(DT)(DG)(DC)(DC) (DT)(DT)(DG)(DG)(DC)(DC)(DA)(DG)(DT)(DT) (DT)(DT)(DC)(DC)(DA) (DT)(DG)(DT)(DA) (DC)(DA)(DT)(DG)(DC)(DA)(DG)(DA)(DA)(DA) (DG)(DA)(DA)(DG)(DT)(DT) (DT)(DG)(DG) (DA)(DC)(DT)(DG)(DA)(DT)(DC)(DA)(DA)(DT) (DA)(DC)(DA)(DG)(DT)(DC)(DC) (DT)(DC) (DT)(DG)(DC)(DC)(DT)(DT)(DT)(DA)(DA)(DA) (DG)(DC)(DA)(DA)(DT)(DA)(DG)(DG) (DA) (DA)(DA)(DG)(DA)(DT)

+
Macromolecule #6: DNA (171-MER)

MacromoleculeName: DNA (171-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 57.42777 KDa
SequenceString: (DA)(DT)(DC)(DT)(DT)(DT)(DC)(DC)(DT)(DA) (DT)(DT)(DG)(DC)(DT)(DT)(DT)(DA)(DA)(DA) (DG)(DG)(DC)(DA)(DG)(DA)(DG)(DG)(DA) (DC)(DT)(DG)(DT)(DA)(DT)(DT)(DG)(DA)(DT) (DC) (DA)(DG)(DT)(DC)(DC)(DA) ...String:
(DA)(DT)(DC)(DT)(DT)(DT)(DC)(DC)(DT)(DA) (DT)(DT)(DG)(DC)(DT)(DT)(DT)(DA)(DA)(DA) (DG)(DG)(DC)(DA)(DG)(DA)(DG)(DG)(DA) (DC)(DT)(DG)(DT)(DA)(DT)(DT)(DG)(DA)(DT) (DC) (DA)(DG)(DT)(DC)(DC)(DA)(DA)(DA) (DC)(DT)(DT)(DC)(DT)(DT)(DT)(DC)(DT)(DG) (DC)(DA) (DT)(DG)(DT)(DA)(DC)(DA)(DT) (DG)(DG)(DA)(DA)(DA)(DA)(DC)(DT)(DG)(DG) (DC)(DC)(DA) (DA)(DG)(DG)(DC)(DA)(DA) (DA)(DC)(DA)(DC)(DG)(DT)(DC)(DC)(DG)(DG) (DA)(DA)(DT)(DG) (DA)(DT)(DG)(DG)(DT) (DA)(DT)(DT)(DT)(DA)(DA)(DG)(DA)(DA)(DC) (DA)(DA)(DA)(DC)(DA) (DT)(DT)(DC)(DC) (DC)(DT)(DG)(DG)(DT)(DA)(DT)(DC)(DA)(DG) (DC)(DA)(DA)(DG)(DT)(DA) (DC)(DA)(DG) (DT)(DG)(DC)(DC)(DC)(DT)(DG)(DC)(DT)(DG) (DA)(DC)(DA)(DG)(DA)(DG)(DC) (DA)(DG) (DG)(DA)(DG)(DA)(DC)(DA)(DC)(DA)(DA)(DA) (DG)(DT)(DA)(DC)(DC)(DA)(DT)(DC) (DT) (DC)(DG)(DG)(DA)(DT)

+
Macromolecule #9: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 9 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 1.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: NONE
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.48 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.1) / Number images used: 403489
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more