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Basic information
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Title | Structure of the human CCAN CENP-A alpha-satellite complex | ||||||||||||
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![]() | Kinetochore / chromosome segregation / centromere / CELL CYCLE | ||||||||||||
Function / homology | ![]() spindle attachment to meiosis I kinetochore / centromeric DNA binding / CENP-A containing chromatin assembly / protein localization to chromosome, centromeric region / kinetochore assembly / attachment of mitotic spindle microtubules to kinetochore / inner kinetochore / condensed chromosome, centromeric region / establishment of mitotic spindle orientation / mitotic cytokinesis ...spindle attachment to meiosis I kinetochore / centromeric DNA binding / CENP-A containing chromatin assembly / protein localization to chromosome, centromeric region / kinetochore assembly / attachment of mitotic spindle microtubules to kinetochore / inner kinetochore / condensed chromosome, centromeric region / establishment of mitotic spindle orientation / mitotic cytokinesis / chromosome, centromeric region / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / pericentric heterochromatin / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / Packaging Of Telomere Ends / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / nucleosomal DNA binding / 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 / Resolution of Sister Chromatid Cohesion / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere organization / RNA Polymerase I Promoter Opening / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / innate immune response in mucosa / PRC2 methylates histones and DNA / Defective pyroptosis / chromosome segregation / HDACs deacetylate histones / RHO GTPases Activate Formins / RNA Polymerase I Promoter Escape / Nonhomologous End-Joining (NHEJ) / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / G2/M DNA damage checkpoint / HDMs demethylate histones / B-WICH complex positively regulates rRNA expression / heterochromatin formation / DNA Damage/Telomere Stress Induced Senescence / Metalloprotease DUBs / 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 / HCMV Early Events / Transcriptional regulation of granulopoiesis / Separation of Sister Chromatids / structural constituent of chromatin / UCH proteinases / antimicrobial humoral immune response mediated by antimicrobial peptide / nucleosome / nucleosome assembly / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromatin organization / mitotic cell cycle / RUNX1 regulates transcription of genes involved in differentiation of HSCs / HATs acetylate histones / antibacterial humoral response / Processing of DNA double-strand break ends / midbody / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / chromosome, telomeric region / nuclear body / Ub-specific processing proteases / defense response to Gram-positive bacterium / protein heterodimerization activity / Amyloid fiber formation / negative regulation of cell population proliferation / cell division / chromatin binding / protein-containing complex / DNA binding / RNA binding / extracellular space / extracellular exosome / extracellular region / nucleoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.68 Å | ||||||||||||
![]() | Yatskevich S / Muir KW | ||||||||||||
Funding support | ![]()
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![]() | ![]() 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 |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 14.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19 KB 19 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.6 KB | Display | ![]() |
Images | ![]() | 81.2 KB | ||
Filedesc metadata | ![]() | 6.3 KB | ||
Others | ![]() | 170.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7piiMC ![]() 7pb4C ![]() 7pb8C ![]() 7pknC ![]() 7r5rC ![]() 7r5sC ![]() 7r5vC ![]() 7ywxC ![]() 7yyhC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.831 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_13437_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : CENP-A nucleosome in complex with CENP-C
Entire | Name: CENP-A nucleosome in complex with CENP-C |
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Components |
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-Supramolecule #1: CENP-A nucleosome in complex with CENP-C
Supramolecule | Name: 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
Macromolecule | Name: Histone H3-like centromeric protein A / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 16.02363 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGPRRRSRKP EAPRRRSPSP TPTPGPSRRG PSLGASSHQH SRRRQGWLKE IRKLQKSTHL LIRKLPFSRL AREICVKFTR GVDFNWQAQ ALLALQEAAE AFLVHLFEDA YLLTLHAGRV TLFPKDVQLA RRIRGLEEGL G UniProtKB: Histone H3-like centromeric protein A |
-Macromolecule #2: Histone H4
Macromolecule | Name: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 11.394426 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG UniProtKB: Histone H4 |
-Macromolecule #3: Histone H2A type 1-C
Macromolecule | Name: Histone H2A type 1-C / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 16.666334 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGSSHHHHHH SPGLEVLFQG PRGMSGRGKQ GGKARAKAKS RSSRAGLQFP VGRVHRLLRK GNYAERVGAG APVYLAAVLE YLTAEILEL AGNAARDNKK TRIIPRHLQL AIRNDEELNK LLGRVTIAQG GVLPNIQAVL LPKKTESHHK AKGK UniProtKB: Histone H2A type 1-C |
-Macromolecule #4: Histone H2B type 1-C/E/F/G/I
Macromolecule | Name: Histone H2B type 1-C/E/F/G/I / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 13.937213 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSSK UniProtKB: Histone H2B type 1-C/E/F/G/I |
-Macromolecule #7: Centromere protein C
Macromolecule | Name: Centromere protein C / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 61.943082 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: 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 |
-Macromolecule #5: DNA (122-MER)
Macromolecule | Name: DNA (122-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 52.747801 KDa |
Sequence | 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) ...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) |
-Macromolecule #6: DNA (123-MER)
Macromolecule | Name: DNA (123-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 52.800816 KDa |
Sequence | 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) ...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) |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |