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- EMDB-13437: Structure of the human CCAN CENP-A alpha-satellite complex -

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Basic information

Entry
Database: EMDB / ID: EMD-13437
TitleStructure of the human CCAN CENP-A alpha-satellite complex
Map data
Sample
  • Complex: CENP-A nucleosome in complex with CENP-C
    • Protein or peptide: Histone H3-like centromeric protein A
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-C
    • Protein or peptide: Histone H2B type 1-C/E/F/G/I
    • DNA: DNA (122-MER)
    • DNA: DNA (123-MER)
    • Protein or peptide: Centromere protein C
KeywordsKinetochore / chromosome segregation / centromere / CELL CYCLE
Function / homology
Function and homology information


spindle attachment to meiosis I kinetochore / CENP-A containing chromatin assembly / centromeric DNA binding / kinetochore assembly / protein localization to chromosome, centromeric region / attachment of mitotic spindle microtubules to kinetochore / condensed chromosome, centromeric region / inner kinetochore / pericentric heterochromatin / mitotic cytokinesis ...spindle attachment to meiosis I kinetochore / CENP-A containing chromatin assembly / centromeric DNA binding / kinetochore assembly / protein localization to chromosome, centromeric region / attachment of mitotic spindle microtubules to kinetochore / condensed chromosome, centromeric region / inner kinetochore / pericentric heterochromatin / mitotic cytokinesis / establishment of mitotic spindle orientation / chromosome, centromeric region / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / Packaging Of Telomere Ends / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / 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 / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / telomere organization / Inhibition of DNA recombination at telomere / RNA Polymerase I Promoter Opening / Meiotic synapsis / Assembly of the ORC complex at the origin of replication / Resolution of Sister Chromatid Cohesion / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / Chromatin modifications during the maternal to zygotic transition (MZT) / SIRT1 negatively regulates rRNA expression / HCMV Late Events / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / innate immune response in mucosa / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / HDMs demethylate histones / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / chromosome segregation / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Nonhomologous End-Joining (NHEJ) / Transcriptional regulation by small RNAs / RHO GTPases Activate Formins / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / G2/M DNA damage checkpoint / Metalloprotease DUBs / NoRC negatively regulates rRNA expression / DNA Damage/Telomere Stress Induced Senescence / B-WICH complex positively regulates rRNA expression / kinetochore / PKMTs methylate histone lysines / Meiotic recombination / Pre-NOTCH Transcription and Translation / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / Transcriptional regulation of granulopoiesis / Separation of Sister Chromatids / UCH proteinases / HCMV Early Events / antimicrobial humoral immune response mediated by antimicrobial peptide / structural constituent of chromatin / antibacterial humoral response / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / nucleosome / heterochromatin formation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / mitotic cell cycle / nucleosome assembly / Processing of DNA double-strand break ends / HATs acetylate histones / Senescence-Associated Secretory Phenotype (SASP) / chromatin organization / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / midbody / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / chromosome, telomeric region / Ub-specific processing proteases / defense response to Gram-positive bacterium / nuclear body / Amyloid fiber formation / protein heterodimerization activity / negative regulation of cell population proliferation / cell division / chromatin binding / protein-containing complex / extracellular space / DNA binding / RNA binding
Similarity search - Function
CENP-C, middle DNMT3B-binding domain / Centromere assembly component CENP-C middle DNMT3B-binding region / Kinetochore assembly subunit CENP-C, N-terminal domain / Kinetochore assembly subunit CENP-C N-terminal / Mif2/CENP-C cupin domain / Centromere protein C/Mif2/cnp3 / Mif2/CENP-C like / RmlC-like cupin domain superfamily / RmlC-like jelly roll fold / : ...CENP-C, middle DNMT3B-binding domain / Centromere assembly component CENP-C middle DNMT3B-binding region / Kinetochore assembly subunit CENP-C, N-terminal domain / Kinetochore assembly subunit CENP-C N-terminal / Mif2/CENP-C cupin domain / Centromere protein C/Mif2/cnp3 / Mif2/CENP-C like / RmlC-like cupin domain superfamily / RmlC-like jelly roll fold / : / 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 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold
Similarity search - Domain/homology
Histone H3-like centromeric protein A / Histone H4 / Histone H2B type 1-C/E/F/G/I / Centromere protein C / Histone H2A type 1-C
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.68 Å
AuthorsYatskevich S / Muir KW
Funding support Germany, 3 items
OrganizationGrant numberCountry
Cancer Research UK Germany
Medical Research Council (MRC, United Kingdom) Germany
Boehringer Ingelheim Fonds (BIF) Germany
CitationJournal: Science / Year: 2022
Title: Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome.
Authors: Stanislau Yatskevich / Kyle W Muir / Dom Bellini / Ziguo Zhang / Jing Yang / Thomas Tischer / Masa Predin / Tom Dendooven / Stephen H McLaughlin / David Barford /
Abstract: Kinetochores assemble onto specialized centromeric CENP-A (centromere protein A) nucleosomes (CENP-A) to mediate attachments between chromosomes and the mitotic spindle. We describe cryo-electron ...Kinetochores assemble onto specialized centromeric CENP-A (centromere protein A) nucleosomes (CENP-A) to mediate attachments between chromosomes and the mitotic spindle. We describe cryo-electron microscopy structures of the human inner kinetochore constitutive centromere associated network (CCAN) complex bound to CENP-A reconstituted onto α-satellite DNA. CCAN forms edge-on contacts with CENP-A, and a linker DNA segment of the α-satellite repeat emerges from the fully wrapped end of the nucleosome to thread through the central CENP-LN channel that tightly grips the DNA. The CENP-TWSX histone-fold module further augments DNA binding and partially wraps the linker DNA in a manner reminiscent of canonical nucleosomes. Our study suggests that the topological entrapment of the linker DNA by CCAN provides a robust mechanism by which kinetochores withstand both pushing and pulling forces exerted by the mitotic spindle.
History
DepositionAug 19, 2021-
Header (metadata) releaseMay 25, 2022-
Map releaseMay 25, 2022-
UpdateJul 17, 2024-
Current statusJul 17, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_13437.png

Downloads & links

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Map

FileDownload / File: emd_13437.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 384 pix.
= 319.104 Å		0.83 Å/pix.
x 384 pix.
= 319.104 Å		0.83 Å/pix.
x 384 pix.
= 319.104 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.831 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0172
Minimum - Maximum-0.06478859 - 0.1361038
Average (Standard dev.)0.00008936151 (±0.0019000238)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 319.104 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_13437_additional_1.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 : CENP-A nucleosome in complex with CENP-C

EntireName: CENP-A nucleosome in complex with CENP-C
Components
  • Complex: CENP-A nucleosome in complex with CENP-C
    • Protein or peptide: Histone H3-like centromeric protein A
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-C
    • Protein or peptide: Histone H2B type 1-C/E/F/G/I
    • DNA: DNA (122-MER)
    • DNA: DNA (123-MER)
    • Protein or peptide: Centromere protein C

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Supramolecule #1: CENP-A nucleosome in complex with CENP-C

SupramoleculeName: CENP-A nucleosome in complex with CENP-C / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7

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Macromolecule #1: Histone H3-like centromeric protein A

MacromoleculeName: Histone H3-like centromeric protein A / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.02363 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGPRRRSRKP EAPRRRSPSP TPTPGPSRRG PSLGASSHQH SRRRQGWLKE IRKLQKSTHL LIRKLPFSRL AREICVKFTR GVDFNWQAQ ALLALQEAAE AFLVHLFEDA YLLTLHAGRV TLFPKDVQLA RRIRGLEEGL G

UniProtKB: Histone H3-like centromeric protein A

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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

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Macromolecule #3: Histone H2A type 1-C

MacromoleculeName: Histone H2A type 1-C / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.666334 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGSSHHHHHH SPGLEVLFQG PRGMSGRGKQ GGKARAKAKS RSSRAGLQFP VGRVHRLLRK GNYAERVGAG APVYLAAVLE YLTAEILEL AGNAARDNKK TRIIPRHLQL AIRNDEELNK LLGRVTIAQG GVLPNIQAVL LPKKTESHHK AKGK

UniProtKB: Histone H2A type 1-C

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Macromolecule #4: Histone H2B type 1-C/E/F/G/I

MacromoleculeName: Histone H2B type 1-C/E/F/G/I / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.937213 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSSK

UniProtKB: Histone H2B type 1-C/E/F/G/I

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Macromolecule #7: Centromere protein C

MacromoleculeName: Centromere protein C / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 61.943082 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAASGLDHLK NGYRRRFCRP SRARDINTEQ GQNVLEILQD CFEEKSLAND FSTNSTKSVP NSTRKIKDTC IQSPSKECQK SHPKSVPVS SKKKEASLQF VVEPSEATNR SVQAHEVHQK ILATDVSSKN TPDSKKISSR NINDHHSEAD EEFYLSVGSP S VLLDAKTS ...String:
MAASGLDHLK NGYRRRFCRP SRARDINTEQ GQNVLEILQD CFEEKSLAND FSTNSTKSVP NSTRKIKDTC IQSPSKECQK SHPKSVPVS SKKKEASLQF VVEPSEATNR SVQAHEVHQK ILATDVSSKN TPDSKKISSR NINDHHSEAD EEFYLSVGSP S VLLDAKTS VSQNVIPSSA QKRETYTFEN SVNMLPSSTE VSVKTKKRLN FDDKVMLKKI EIDNKVSDEE DKTSEGQERK PS GSSQNRI RDSEYEIQRQ AKKSFSTLFL ETVKRKSESS PIVRHAATAP PHSCPPDDTK LIEDEFIIDE SDQSFASRSW ITI PRKAGS LKQRTISPAE STALLQGRKS REKHHNILPK TLANDKHSHK PHPVETSQPS DKTVLDTSYA LIGETVNNYR STKY EMYSK NAEKPSRSKR TIKQKQRRKF MAKPAEEQLD VGQSKDENIH TSHITQDEFQ RNSDRNMEEH EEMGNDCVSK KQMPP VGSK KSSTRKDKEE SKKKRFSSES KNKLVPEEVT STVTKSRRIS RRPSDWWVVK SEESPVYSNS S

UniProtKB: Centromere protein C

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Macromolecule #5: DNA (122-MER)

MacromoleculeName: DNA (122-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.747801 KDa
SequenceString: (DC)(DT)(DA)(DC)(DA)(DA)(DA)(DA)(DA)(DG) (DA)(DG)(DT)(DG)(DT)(DT)(DT)(DC)(DA)(DA) (DA)(DA)(DC)(DT)(DG)(DC)(DT)(DC)(DT) (DA)(DT)(DC)(DA)(DA)(DA)(DA)(DG)(DG)(DA) (DA) (DT)(DG)(DT)(DT)(DC)(DA) ...String:
(DC)(DT)(DA)(DC)(DA)(DA)(DA)(DA)(DA)(DG) (DA)(DG)(DT)(DG)(DT)(DT)(DT)(DC)(DA)(DA) (DA)(DA)(DC)(DT)(DG)(DC)(DT)(DC)(DT) (DA)(DT)(DC)(DA)(DA)(DA)(DA)(DG)(DG)(DA) (DA) (DT)(DG)(DT)(DT)(DC)(DA)(DA)(DC) (DT)(DC)(DT)(DG)(DT)(DG)(DA)(DG)(DT)(DT) (DG)(DA) (DA)(DT)(DG)(DC)(DA)(DA)(DT) (DC)(DA)(DT)(DC)(DA)(DC)(DA)(DA)(DA)(DG) (DA)(DA)(DG) (DT)(DT)(DT)(DC)(DT)(DG) (DA)(DG)(DA)(DA)(DT)(DG)(DC)(DT)(DT)(DC) (DT)(DG)(DT)(DT) (DT)(DA)(DG)(DT)(DT) (DT)(DT)(DT)(DA)(DT)(DG)(DT)(DG)(DA)(DA) (DG)(DA)(DT)(DA)(DT) (DT)(DC)(DC)(DC) (DG)(DT)(DT)(DT)(DC)(DC)(DA)(DA)(DC)(DG) (DA)(DA)(DG)(DG)(DC)(DC) (DT)(DC)(DA) (DA)(DA)(DG)(DC)(DG)(DG)(DT)(DC)(DC)(DA) (DA)(DA)(DT)(DA)(DT)(DC)(DC) (DA)(DC) (DT)(DT)(DG)(DC)(DA)(DG)(DA)(DT)(DT)

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Macromolecule #6: DNA (123-MER)

MacromoleculeName: DNA (123-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.800816 KDa
SequenceString: (DA)(DA)(DT)(DC)(DT)(DG)(DC)(DA)(DA)(DG) (DT)(DG)(DG)(DA)(DT)(DA)(DT)(DT)(DT)(DG) (DG)(DA)(DC)(DC)(DG)(DC)(DT)(DT)(DT) (DG)(DA)(DG)(DG)(DC)(DC)(DT)(DT)(DC)(DG) (DT) (DT)(DG)(DG)(DA)(DA)(DA) ...String:
(DA)(DA)(DT)(DC)(DT)(DG)(DC)(DA)(DA)(DG) (DT)(DG)(DG)(DA)(DT)(DA)(DT)(DT)(DT)(DG) (DG)(DA)(DC)(DC)(DG)(DC)(DT)(DT)(DT) (DG)(DA)(DG)(DG)(DC)(DC)(DT)(DT)(DC)(DG) (DT) (DT)(DG)(DG)(DA)(DA)(DA)(DC)(DG) (DG)(DG)(DA)(DA)(DT)(DA)(DT)(DC)(DT)(DT) (DC)(DA) (DC)(DA)(DT)(DA)(DA)(DA)(DA) (DA)(DC)(DT)(DA)(DA)(DA)(DC)(DA)(DG)(DA) (DA)(DG)(DC) (DA)(DT)(DT)(DC)(DT)(DC) (DA)(DG)(DA)(DA)(DA)(DC)(DT)(DT)(DC)(DT) (DT)(DT)(DG)(DT) (DG)(DA)(DT)(DG)(DA) (DT)(DT)(DG)(DC)(DA)(DT)(DT)(DC)(DA)(DA) (DC)(DT)(DC)(DA)(DC) (DA)(DG)(DA)(DG) (DT)(DT)(DG)(DA)(DA)(DC)(DA)(DT)(DT)(DC) (DC)(DT)(DT)(DT)(DT)(DG) (DA)(DT)(DA) (DG)(DA)(DG)(DC)(DA)(DG)(DT)(DT)(DT)(DT) (DG)(DA)(DA)(DA)(DC)(DA)(DC) (DT)(DC) (DT)(DT)(DT)(DT)(DT)(DG)(DT)(DA)(DG)

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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: 7.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.68 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1093274
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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